RPS6KA1

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Ribosomal protein S6 kinase, 90kDa, polypeptide 1

Identifiers

RPS6KA1; HU-1; MAPKAPK1A; RSK; RSK1; S6K-alpha 1

External IDs

OMIM: 601684 MGI: 104558 HomoloGene: 55703

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • protein serine/threonine kinase activity • protein binding • ATP binding • transferase activity
Biological Process:	• protein amino acid phosphorylation • signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001006665 (mRNA)
NP_001006666 (protein)

NM_009097 (mRNA)
NP_033123 (protein)

Location

Chr 1: 26.73 - 26.77 Mb

Chr 4: 133.12 - 133.16 Mb

Pubmed search

[1]

[2]

Ribosomal protein S6 kinase, 90kDa, polypeptide 1, also known as RPS6KA1, is a human gene.

This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 nonidentical 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. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.^[1]

[edit] See also

Ribosomal s6 kinase

[edit] References

^ Entrez Gene: RPS6KA1 ribosomal protein S6 kinase, 90kDa, polypeptide 1.

[edit] Further reading

Chen RH, Sarnecki C, Blenis J (1992). "Nuclear localization and regulation of erk- and rsk-encoded protein kinases.". Mol. Cell. Biol. 12 (3): 915–27. PMID 1545823.
Tratner I, Ofir R, Verma IM (1992). "Alteration of a cyclic AMP-dependent protein kinase phosphorylation site in the c-Fos protein augments its transforming potential.". Mol. Cell. Biol. 12 (3): 998–1006. PMID 1545828.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Moller DE, Xia CH, Tang W, et al. (1994). "Human rsk isoforms: cloning and characterization of tissue-specific expression.". Am. J. Physiol. 266 (2 Pt 1): C351–9. PMID 8141249.
Chen RH, Abate C, Blenis J (1994). "Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase.". Proc. Natl. Acad. Sci. U.S.A. 90 (23): 10952–6. PMID 8248197.
Rivera VM, Miranti CK, Misra RP, et al. (1993). "A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity.". Mol. Cell. Biol. 13 (10): 6260–73. PMID 8413226.
Chen ZJ, Parent L, Maniatis T (1996). "Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity.". Cell 84 (6): 853–62. PMID 8601309.
Barge RM, de Koning JP, Pouwels K, et al. (1996). "Tryptophan 650 of human granulocyte colony-stimulating factor (G-CSF) receptor, implicated in the activation of JAK2, is also required for G-CSF-mediated activation of signaling complexes of the p21ras route.". Blood 87 (6): 2148–53. PMID 8630373.
Wong EV, Schaefer AW, Landreth G, Lemmon V (1996). "Involvement of p90rsk in neurite outgrowth mediated by the cell adhesion molecule L1.". J. Biol. Chem. 271 (30): 18217–23. PMID 8663493.
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): 959–63. PMID 8688081.
Nakajima T, Fukamizu A, Takahashi J, et al. (1996). "The signal-dependent coactivator CBP is a nuclear target for pp90RSK.". Cell 86 (3): 465–74. PMID 8756728.
Zhao Y, Bjorbaek C, Moller DE (1997). "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases.". J. Biol. Chem. 271 (47): 29773–9. PMID 8939914.
Zaheer A, Lim R (1997). "Protein kinase A (PKA)- and protein kinase C-phosphorylated glia maturation factor promotes the catalytic activity of PKA.". J. Biol. Chem. 272 (8): 5183–6. PMID 9030586.
Schouten GJ, Vertegaal AC, Whiteside ST, et al. (1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase.". EMBO J. 16 (11): 3133–44. doi:10.1093/emboj/16.11.3133. PMID 9214631.
Li HL, Forman MS, Kurosaki T, Puré E (1997). "Syk is required for BCR-mediated activation of p90Rsk, but not p70S6k, via a mitogen-activated protein kinase-independent pathway in B cells.". J. Biol. Chem. 272 (29): 18200–8. PMID 9218456.
Chang YW, Traugh JA (1997). "Phosphorylation of elongation factor 1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation.". J. Biol. Chem. 272 (45): 28252–7. PMID 9353277.
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): 149–56. PMID 9373149.
del Peso L, González-García M, Page C, et al. (1997). "Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt.". Science 278 (5338): 687–9. PMID 9381178.
Dalby KN, Morrice N, Caudwell FB, et al. (1998). "Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.". J. Biol. Chem. 273 (3): 1496–505. PMID 9430688.
Joel PB, Smith J, Sturgill TW, et al. (1998). "pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167.". Mol. Cell. Biol. 18 (4): 1978–84. PMID 9528769.