RPS6KA3

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Ribosomal protein S6 kinase, 90kDa, polypeptide 3
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols RPS6KA3 ; CLS; HU-3; ISPK-1; MAPKAPK1B; MRX19; RSK; RSK2; S6K-alpha3; p90-RSK2; pp90RSK2
External IDs OMIM300075 MGI104557 HomoloGene37940 ChEMBL: 2345 GeneCards: RPS6KA3 Gene
EC number 2.7.11.1
RNA expression pattern
PBB GE RPS6KA3 203843 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6197 110651
Ensembl ENSG00000177189 ENSMUSG00000031309
UniProt P51812 P18654
RefSeq (mRNA) NM_004586 NM_148945
RefSeq (protein) NP_004577 NP_683747
Location (UCSC) Chr X:
20.17 – 20.29 Mb
Chr X:
159.21 – 159.37 Mb
PubMed search [1] [2]

Ribosomal protein S6 kinase, 90kDa, polypeptide 3, also known as RPS6KA3, is an enzyme that in humans is encoded by the RPS6KA3 gene.[1][2]

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.[1]

Clinical significance[edit]

Mutations in this gene have been associated with Coffin-Lowry syndrome (CLS).[3]

Interactions[edit]

RPS6KA3 has been shown to interact with CREB-binding protein,[4] MAPK1[5][6] and PEA15.[7]

References[edit]

  1. ^ a b "Entrez Gene: RPS6KA3 ribosomal protein S6 kinase, 90kDa, polypeptide 3". 
  2. ^ 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. 
  3. ^ 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. 
  4. ^ 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 99884. PMID 11564891. 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ 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]