RPS6KA4

Ribosomal protein S6 kinase, 90kDa, polypeptide 4
Identifiers
Symbols	RPS6KA4; MSK2; RSK-B
External IDs	OMIM: 603606 MGI: 1930076 HomoloGene: 69288 ChEMBL: 3125 GeneCards: RPS6KA4 Gene
EC number	2.7.11.1
Gene Ontology Molecular function • magnesium ion binding • protein serine/threonine kinase activity • ribosomal protein S6 kinase activity • protein binding • ATP binding • mitogen-activated protein kinase p38 binding Cellular component • nucleus • nucleolus • cytoplasm Biological process • negative regulation of cytokine production • regulation of transcription, DNA-dependent • protein phosphorylation • inflammatory response • intracellular protein kinase cascade • axon guidance • histone phosphorylation • positive regulation of CREB transcription factor activity • positive regulation of histone phosphorylation • positive regulation of histone acetylation • histone H3-S10 phosphorylation • histone H3-S28 phosphorylation • positive regulation of transcription from RNA polymerase II promoter • positive regulation of NF-kappaB transcription factor activity • interleukin-1-mediated signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8986	56613
Ensembl	ENSG00000162302	ENSMUSG00000024952
UniProt	O75676	Q9Z2B9
RefSeq (mRNA)	NM_001006944	NM_019924
RefSeq (protein)	NP_001006945	NP_064308
Location (UCSC)	Chr 11: 64.13 – 64.14 Mb	Chr 19: 6.83 – 6.84 Mb
PubMed search	[1]	[2]

Ribosomal protein S6 kinase alpha-4 is an enzyme that in humans is encoded by the RPS6KA4 gene.

Function

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 CREB1 and c-Fos. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.

Interactions

RPS6KA4 has been shown to interact with MAPK14.

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• 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): 959–963. doi:10.1126/science.273.5277.959. PMID 8688081. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Du K, Montminy M (1999). "CREB is a regulatory target for the protein kinase Akt/PKB". J. Biol. Chem. 273 (49): 32377–32379. doi:10.1074/jbc.273.49.32377. PMID 9829964. 
• Zhu S, Gerhard DS (1999). "A transcript map of an 800-kb region on human chromosome 11q13, part of the candidate region for SCA5 and BBS1". Hum. Genet. 103 (6): 674–680. doi:10.1007/s004390050890. PMID 9921902. 
• Tomás-Zuber M, Mary JL, Lesslauer W (2000). "Control sites of ribosomal S6 kinase B and persistent activation through tumor necrosis factor". J. Biol. Chem. 275 (31): 23549–23558. doi:10.1074/jbc.M002586200. PMID 10806207. 
• Tomás-Zuber M, Mary JL, Lamour F et al. (2001). "C-terminal elements control location, activation threshold, and p38 docking of ribosomal S6 kinase B (RSKB)". J. Biol. Chem. 276 (8): 5892–5899. doi:10.1074/jbc.M005822200. PMID 11035004. 
• 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): 6324–6333. doi:10.1038/sj.onc.1204007. PMID 11175347. 
• Prymakowska-Bosak M, Misteli T, Herrera JE et al. (2001). "Mitotic phosphorylation prevents the binding of HMGN proteins to chromatin". Mol. Cell. Biol. 21 (15): 5169–5178. doi:10.1128/MCB.21.15.5169-5178.2001. PMC 87241. PMID 11438671. 
• 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): 2871–2881. doi:10.1128/MCB.22.8.2871-2881.2002. PMC 133730. PMID 11909979. 
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
• Soloaga A, Thomson S, Wiggin GR et al. (2003). "MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14". EMBO J. 22 (11): 2788–2797. doi:10.1093/emboj/cdg273. PMC 156769. PMID 12773393. 
• Wissing J, Jänsch L, Nimtz M et al. (2007). "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry". Mol. Cell Proteomics 6 (3): 537–547. doi:10.1074/mcp.T600062-MCP200. PMID 17192257. 
• Gesser B, Johansen C, Rasmussen MK et al. (2007). "Dimethylfumarate specifically inhibits the mitogen and stress-activated kinases 1 and 2 (MSK1/2): possible role for its anti-psoriatic effect". J. Invest. Dermatol. 127 (9): 2129–2137. doi:10.1038/sj.jid.5700859. PMID 17495961.