RPS6KA3

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RPS6KA3
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases RPS6KA3, CLS, HU-3, ISPK-1, MAPKAPK1B, MRX19, RSK, RSK2, S6K-alpha3, p90-RSK2, pp90RSK2, ribosomal protein S6 kinase A3
External IDs MGI: 104557 HomoloGene: 37940 GeneCards: RPS6KA3
RNA expression pattern
PBB GE RPS6KA3 203843 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004586

NM_148945
NM_001346675

RefSeq (protein)

NP_004577

NP_683747.1
NP_001333604
NP_683747

Location (UCSC) Chr X: 20.15 – 20.27 Mb Chr X: 159.21 – 159.37 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Ribosomal protein S6 kinase, 90kDa, polypeptide 3, also known as RPS6KA3, is an enzyme that in humans is encoded by the RPS6KA3 gene.[3][4]

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.[3]

Clinical significance[edit]

Mutations in this gene have been associated with Coffin–Lowry syndrome (CLS).[5]

Interactions[edit]

RPS6KA3 has been shown to interact with CREB-binding protein,[6] MAPK1[7][8] and PEA15.[9]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b "Entrez Gene: RPS6KA3 ribosomal protein S6 kinase, 90kDa, polypeptide 3". 
  4. ^ Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M (February 1994). "Human rsk isoforms: cloning and characterization of tissue-specific expression". Am. J. Physiol. 266 (2 Pt 1): C351–9. PMID 8141249. 
  5. ^ 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)". Eur. J. Hum. Genet. 10 (1): 2–5. doi:10.1038/sj.ejhg.5200738. PMID 11896450. 
  6. ^ Merienne, K; Pannetier S; Harel-Bellan A; Sassone-Corsi P (October 2001). "Mitogen-Regulated RSK2-CBP Interaction Controls Their Kinase and Acetylase Activities". Mol. Cell. Biol. United States. 21 (20): 7089–96. doi:10.1128/MCB.21.20.7089-7096.2001. ISSN 0270-7306. PMC 99884Freely accessible. PMID 11564891. 
  7. ^ Zhao, Y; Bjorbaek C; Moller D E (November 1996). "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases". J. Biol. Chem. UNITED STATES. 271 (47): 29773–9. doi:10.1074/jbc.271.47.29773. ISSN 0021-9258. PMID 8939914. 
  8. ^ Smith, J A; Poteet-Smith C E; Malarkey K; Sturgill T W (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". J. Biol. Chem. UNITED STATES. 274 (5): 2893–8. doi:10.1074/jbc.274.5.2893. ISSN 0021-9258. PMID 9915826. 
  9. ^ Vaidyanathan, Hema; Ramos Joe W (August 2003). "RSK2 activity is regulated by its interaction with PEA-15". J. Biol. Chem. United States. 278 (34): 32367–72. doi:10.1074/jbc.M303988200. ISSN 0021-9258. PMID 12796492. 

Further reading[edit]

External links[edit]