RPS6KA5

Enzyme
RPS6KA5
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1VZO, 3KN5, 3KN6

Identifiers
AliasesRPS6KA5, MSK1, MSPK1, RLPK, ribosomal protein S6 kinase A5
External IDsOMIM: 603607; MGI: 1920336; HomoloGene: 48302; GeneCards: RPS6KA5; OMA:RPS6KA5 - orthologs
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for RPS6KA5
Genomic location for RPS6KA5
Band14q32.11Start90,847,861 bp[1]
End91,060,641 bp[1]
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[2]
Chromosome 12 (mouse)
Genomic location for RPS6KA5
Genomic location for RPS6KA5
Band12|12 EStart100,514,698 bp[2]
End100,693,242 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • nipple

  • corpus callosum

  • inferior ganglion of vagus nerve

  • Brodmann area 23

  • pons

  • bronchial epithelial cell

  • lactiferous duct

  • body of tongue

  • orbitofrontal cortex
Top expressed in
  • olfactory tubercle

  • secondary oocyte

  • cerebellar vermis

  • nucleus accumbens

  • subiculum

  • spermatid

  • suprachiasmatic nucleus

  • extraocular muscle

  • globus pallidus

  • amygdala
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • protein kinase activity
  • nucleotide binding
  • metal ion binding
  • kinase activity
  • protein binding
  • ATP binding
  • magnesium ion binding
  • protein serine/threonine kinase activity
Cellular component
  • cytoplasm
  • nucleoplasm
  • nucleus
Biological process
  • intracellular signal transduction
  • regulation of transcription, DNA-templated
  • epidermal growth factor receptor signaling pathway
  • phosphorylation
  • stimulatory C-type lectin receptor signaling pathway
  • axon guidance
  • positive regulation of histone acetylation
  • interleukin-1-mediated signaling pathway
  • protein phosphorylation
  • positive regulation of CREB transcription factor activity
  • positive regulation of NF-kappaB transcription factor activity
  • inflammatory response
  • negative regulation of transcription, DNA-templated
  • negative regulation of cytokine production
  • positive regulation of transcription by RNA polymerase II
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9252

73086

Ensembl

ENSG00000100784

ENSMUSG00000021180

UniProt

O75582

Q8C050

RefSeq (mRNA)
NM_004755
NM_182398
NM_001322227
NM_001322228
NM_001322229

NM_001322230
NM_001322231
NM_001322232
NM_001322233
NM_001322234
NM_001322235
NM_001322236
NM_001322237
NM_001322238

NM_153587
NM_001330702

RefSeq (protein)
NP_001309156
NP_001309157
NP_001309158
NP_001309159
NP_001309160

NP_001309161
NP_001309162
NP_001309163
NP_001309164
NP_001309165
NP_001309166
NP_001309167
NP_004746
NP_872198

NP_001317631
NP_705815

Location (UCSC)Chr 14: 90.85 – 91.06 MbChr 12: 100.51 – 100.69 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ribosomal protein S6 kinase alpha-5 is an enzyme that in humans is encoded by the RPS6KA5 gene.[5][6][7] This kinase, together with RPS6KA4, are thought to mediate the phosphorylation of histone H3, linked to the expression of immediate early genes.[8][9]

Interactions

RPS6KA5 has been shown to interact with CREB1.[5][10]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100784 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021180 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Deak M, Clifton AD, Lucocq LM, Alessi DR (September 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.
  6. ^ Jiang C, Yu L, Tu Q, Zhao Y, Zhang H, Zhao S (April 2000). "Assignment of a member of the ribosomal protein S6 kinase family, RPS6KA5, to human chromosome 14q31→q32.1 by radiation hybrid mapping". Cytogenet Cell Genet. 87 (3–4): 261–2. doi:10.1159/000015441. PMID 10702687. S2CID 10527498.
  7. ^ "Entrez Gene: RPS6KA5 ribosomal protein S6 kinase, 90kDa, polypeptide 5".
  8. ^ Soloaga, Ana; Thomson, Stuart; Wiggin, Giselle R.; Rampersaud, Navita; Dyson, Mark H.; Hazzalin, Catherine A.; Mahadevan, Louis C.; Arthur, J.Simon C. (2003-06-02). "MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14". The EMBO Journal. 22 (11): 2788–2797. doi:10.1093/emboj/cdg273. ISSN 0261-4189. PMC 156769. PMID 12773393.
  9. ^ Reul, Johannes M. H. M.; Chandramohan, Yalini (2007-08-01). "Epigenetic mechanisms in stress-related memory formation". Psychoneuroendocrinology. Integrative approaches to neural plasticity (Lille Summer School, 2006). 32: S21–S25. doi:10.1016/j.psyneuen.2007.03.016. ISSN 0306-4530. PMID 17644269. S2CID 24217924.
  10. ^ Wang, X; Li W; Williams M; Terada N; Alessi D R; Proud C G (August 2001). "Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase". EMBO J. 20 (16): 4370–9. doi:10.1093/emboj/20.16.4370. ISSN 0261-4189. PMC 125559. PMID 11500364.

Further reading

  • Chung J, Uchida E, Grammer TC, Blenis J (1997). "STAT3 serine phosphorylation by ERK-dependent and -independent pathways negatively modulates its tyrosine phosphorylation". Mol. Cell. Biol. 17 (11): 6508–16. doi:10.1128/MCB.17.11.6508. PMC 232504. PMID 9343414.
  • Jain N, Zhang T, Fong SL, et al. (1999). "Repression of Stat3 activity by activation of mitogen-activated protein kinase (MAPK)". Oncogene. 17 (24): 3157–67. doi:10.1038/sj.onc.1202238. PMID 9872331.
  • New L, Zhao M, Li Y, et al. (1999). "Cloning and characterization of RLPK, a novel RSK-related protein kinase". J. Biol. Chem. 274 (2): 1026–32. doi:10.1074/jbc.274.2.1026. PMID 9873047.
  • Thomson S, Clayton AL, Hazzalin CA, et al. (1999). "The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase". EMBO J. 18 (17): 4779–93. doi:10.1093/emboj/18.17.4779. PMC 1171550. PMID 10469656.
  • Lim CP, Cao X (1999). "Serine phosphorylation and negative regulation of Stat3 by JNK". J. Biol. Chem. 274 (43): 31055–61. doi:10.1074/jbc.274.43.31055. PMID 10521505.
  • Buck M, Poli V, van der Geer P, et al. (2000). "Phosphorylation of rat serine 105 or mouse threonine 217 in C/EBP beta is required for hepatocyte proliferation induced by TGF alpha". Mol. Cell. 4 (6): 1087–92. doi:10.1016/S1097-2765(00)80237-3. PMID 10635333.
  • 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.
  • Hefner Y, Borsch-Haubold AG, Murakami M, et al. (2001). "Serine 727 phosphorylation and activation of cytosolic phospholipase A2 by MNK1-related protein kinases". J. Biol. Chem. 275 (48): 37542–51. doi:10.1074/jbc.M003395200. PMID 10978317.{{cite journal}}: CS1 maint: numeric names: authors list (link)
  • Arthur JS, Cohen P (2000). "MSK1 is required for CREB phosphorylation in response to mitogens in mouse embryonic stem cells". FEBS Lett. 482 (1–2): 44–8. doi:10.1016/S0014-5793(00)02031-7. PMID 11018520.
  • Sapkota GP, Kieloch A, Lizcano JM, et al. (2001). "Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell vrowth". J. Biol. Chem. 276 (22): 19469–82. doi:10.1074/jbc.M009953200. PMID 11297520.
  • Deb A, Zamanian-Daryoush M, Xu Z, et al. (2001). "Protein kinase PKR is required for platelet-derived growth factor signaling of c-fos gene expression via Erks and Stat3". EMBO J. 20 (10): 2487–96. doi:10.1093/emboj/20.10.2487. PMC 125453. PMID 11350938.
  • Liu G, Zhang Y, Bode AM, et al. (2002). "Phosphorylation of 4E-BP1 is mediated by the p38/MSK1 pathway in response to UVB irradiation". J. Biol. Chem. 277 (11): 8810–6. doi:10.1074/jbc.M110477200. PMID 11777913.
  • Wiggin GR, Soloaga A, Foster JM, et al. (2002). "MSK1 and MSK2 Are Required for the Mitogen- and Stress-Induced Phosphorylation of CREB and ATF1 in Fibroblasts". Mol. Cell. Biol. 22 (8): 2871–81. doi:10.1128/MCB.22.8.2871-2881.2002. PMC 133730. PMID 11909979.
  • Markou T, Lazou A (2002). "Phosphorylation and activation of mitogen- and stress-activated protein kinase-1 in adult rat cardiac myocytes by G-protein-coupled receptor agonists requires both extracellular-signal-regulated kinase and p38 mitogen-activated protein kinase". Biochem. J. 365 (Pt 3): 757–63. doi:10.1042/BJ20011828. PMC 1222733. PMID 11994045.
  • Toska K, Kleppe R, Armstrong CG, et al. (2002). "Regulation of tyrosine hydroxylase by stress-activated protein kinases". J. Neurochem. 83 (4): 775–83. doi:10.1046/j.1471-4159.2002.01172.x. PMID 12421349.
  • 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): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Janknecht R (2003). "Regulation of the ER81 transcription factor and its coactivators by mitogen- and stress-activated protein kinase 1 (MSK1)". Oncogene. 22 (5): 746–55. doi:10.1038/sj.onc.1206185. PMID 12569367. S2CID 30183941.
  • Dolled-Filhart M, Camp RL, Kowalski DP, et al. (2003). "Tissue microarray analysis of signal transducers and activators of transcription 3 (Stat3) and phospho-Stat3 (Tyr705) in node-negative breast cancer shows nuclear localization is associated with a better prognosis". Clin. Cancer Res. 9 (2): 594–600. PMID 12576423.
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  • 1vzo: THE STRUCTURE OF THE N-TERMINAL KINASE DOMAIN OF MSK1 REVEALS A NOVEL AUTOINHIBITORY CONFORMATION FOR A DUAL KINASE PROTEIN
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(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)
MAP2K
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