RPS6KA1

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Ribosomal protein S6 kinase, 90kDa, polypeptide 1

Rendering based on PDB 2WNT.

Available structures
PDB	2WNT, 2Z7Q, 2Z7R, 2Z7S

Identifiers

Symbols

RPS6KA1; HU-1; MAPKAPK1A; RSK; RSK1

External IDs

OMIM: 601684 MGI: 104558 HomoloGene: 55703 GeneCards: RPS6KA1 Gene

EC number

2.7.11.1

Gene Ontology
Molecular function	• nucleotide binding • magnesium ion binding • protein serine/threonine kinase activity • protein binding • ATP binding • kinase activity • caspase inhibitor activity
Cellular component	• nucleoplasm • nucleoplasm • cytosol
Biological process	• toll-like receptor signaling pathway • MyD88-dependent toll-like receptor signaling pathway • MyD88-dependent toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • signal transduction • intracellular protein kinase cascade • synaptic transmission • axon guidance • Toll signaling pathway • phosphorylation • toll-like receptor 1 signaling pathway • toll-like receptor 2 signaling pathway • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • negative regulation of caspase activity • innate immune response • nerve growth factor receptor signaling pathway • stress-activated MAPK cascade
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
26.86 – 26.9 Mb

Chr 4:
133.4 – 133.44 Mb

PubMed search

[1]

[2]

Ribosomal protein S6 kinase alpha-1 is an enzyme that in humans is encoded by the RPS6KA1 gene.^[1]

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.^[2]

1 Interactions
2 See also
3 References
4 Further reading

Interactions

RPS6KA1 has been shown to interact with YWHAB,^[3] MAPK1,^[4]^[5]^[6] IκBα,^[7] TOB1^[8] and TSC2.^[9]^[10]

References

^ Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M (Apr 1994). "Human rsk isoforms: cloning and characterization of tissue-specific expression". Am J Physiol 266 (2 Pt 1): C351–9. PMID 8141249.
^ "Entrez Gene: RPS6KA1 ribosomal protein S6 kinase, 90kDa, polypeptide 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6195.
^ Cavet, Megan E; Lehoux Stephanie, Berk Bradford C (May. 2003). "14-3-3beta is a p90 ribosomal S6 kinase (RSK) isoform 1-binding protein that negatively regulates RSK kinase activity". J. Biol. Chem. (United States) 278 (20): 18376–83. doi:10.1074/jbc.M208475200. ISSN 0021-9258. PMID 12618428.
^ Roux, Philippe P; Richards Stephanie A, Blenis John (Jul. 2003). "Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity". Mol. Cell. Biol. (United States) 23 (14): 4796–804. doi:10.1128/MCB.23.14.4796-4804.2003. ISSN 0270-7306. PMC 162206. PMID 12832467. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=162206.
^ Eblen, Scott T; Kumar N Vinay, Shah Kavita, Henderson Michelle J, Watts Colin K W, Shokat Kevan M, Weber Michael J (Apr. 2003). "Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs". J. Biol. Chem. (United States) 278 (17): 14926–35. doi:10.1074/jbc.M300485200. ISSN 0021-9258. PMID 12594221.
^ Smith, J A; Poteet-Smith C E, Malarkey K, Sturgill T W (Jan. 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.
^ Schouten, G J; Vertegaal A C, Whiteside S T, Israël A, Toebes M, Dorsman J C, van der Eb A J, Zantema A (Jun. 1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase". EMBO J. (ENGLAND) 16 (11): 3133–44. doi:10.1093/emboj/16.11.3133. ISSN 0261-4189. PMC 1169932. PMID 9214631. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169932.
^ Suzuki, T; Matsuda S, Tsuzuku J K, Yoshida Y, Yamamoto T (Feb. 2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob". Genes Cells (England) 6 (2): 131–8. doi:10.1046/j.1365-2443.2001.00406.x. ISSN 1356-9597. PMID 11260258.
^ Roux, Philippe P; Ballif Bryan A, Anjum Rana, Gygi Steven P, Blenis John (Sep. 2004). "Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase". Proc. Natl. Acad. Sci. U.S.A. (United States) 101 (37): 13489–94. doi:10.1073/pnas.0405659101. ISSN 0027-8424. PMC 518784. PMID 15342917. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=518784.
^ Rolfe, Mark; McLeod Laura E, Pratt Phillip F, Proud Christopher G (Jun. 2005). "Activation of protein synthesis in cardiomyocytes by the hypertrophic agent phenylephrine requires the activation of ERK and involves phosphorylation of tuberous sclerosis complex 2 (TSC2)". Biochem. J. (England) 388 (Pt 3): 973–84. doi:10.1042/BJ20041888. PMC 1183479. PMID 15757502. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1183479.

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. PMC 369523. PMID 1545823. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=369523.
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. PMC 369532. PMID 1545828. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=369532.
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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
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. doi:10.1073/pnas.90.23.10952. PMC 47899. PMID 8248197. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=47899.
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. PMC 364685. PMID 8413226. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=364685.
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. doi:10.1016/S0092-8674(00)81064-8. 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. doi:10.1074/jbc.271.30.18217. 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. doi:10.1126/science.273.5277.959. 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. doi:10.1016/S0092-8674(00)80119-1. 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. doi:10.1074/jbc.271.47.29773. 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. doi:10.1074/jbc.272.8.5183. 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. PMC 1169932. PMID 9214631. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169932.
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. doi:10.1074/jbc.272.29.18200. 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. doi:10.1074/jbc.272.45.28252. 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. doi:10.1016/S0378-1119(97)00411-3. 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. doi:10.1126/science.278.5338.687. 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. doi:10.1074/jbc.273.3.1496. 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. PMC 121427. PMID 9528769. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=121427.

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1, LATS2, MAST1, MAST2, STK38, STK38L, CIT, ROCK1, SGK, SGK2, SGK3, Protein kinase B (AKT1, AKT2, AKT3), Ataxia telangiectasia mutated, Mammalian target of rapamycin, EIF-2 kinases (PKR, HRI, EIF2AK3, EIF2AK4), Wee1 (WEE1)

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1, PDK2, PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α (PRKAA1, PRKAA2) · β (PRKAB1, PRKAB2) · γ (PRKAG1, PRKAG2, PRKAG3)

(3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)) (EC 2.7.11.4)	BCKDK, BCKDHA, BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2, IDH3A, IDH3B, IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase (Aurora A kinase, Aurora B kinase)

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK, STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK, IKK2, TBK1, IKBKE, IKBKG, IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A, PRKACG, PRKACB, PRKACA, PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G, PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C, Protein kinase Cζ, PKC alpha, PRKCB1, PRKCD, PRKCE, PRKCH, PRKCG, PRKCI, PRKCQ, Protein kinase N1, PKN2, PKN3,

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase, Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4, GRK5, GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2, CAMK1, CAMK2A, CAMK2B, CAMK2D, CAMK2G, CAMK4, MLCK, CASK, CHEK1, CHEK2, DAPK1, DAPK2, DAPK3, STK11, MAPKAPK2, MAPKAPK3, MAPKAPK5, MARK1, MARK2, MARK3, MARK4, MELK, MKNK1, MKNK2, NUAK1, NUAK2, OBSCN, PASK, PHKG1, PHKG2, PIM1, PIM2, PKD1, PRKD2, PRKD3, PSKH1, SNF1LK2, KIAA0999, STK40, SNF1LK, SNRK, SPEG, TSSK2, Kalirin, TRIB1, TRIB2, TRIB3, TRIO, Titin, DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK, MYLK2, MYLK3, MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1, PHKA2, PHKB, PHKG1, PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K, STK19

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1, PLK2, PLK3, PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1, CDK2, CDKL2, CDK3, CDK4, CDK5, CDKL5, CDK6, CDK7, CDK8, CDK9, CDK10, CDC2L5, CRKRS, PCTK1, PCTK2, PCTK3, PFTK1, CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5, RPS6KA4, P70S6 kinase, P70-S6 Kinase 1, RPS6KB2, RPS6KA2, RPS6KA3, RPS6KA1, RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated (MAPK1, MAPK3, MAPK4, MAPK6, MAPK7, MAPK12, MAPK15), C-Jun N-terminal (MAPK8, MAPK9, MAPK10), P38 mitogen-activated protein (MAPK11, MAPK13, MAPK14)

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases (MAP3K1, MAP3K2, MAP3K3, MAP3K4, MAP3K5, MAP3K6, MAP3K7, MAP3K8) RAFs (ARAF, BRAF, KSR1, KSR2), MLKs (MAP3K12, MAP3K13, MAP3K9, MAP3K10, MAP3K11, MAP3K7, ZAK), CDC7, MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1, TTK, GSK-3

(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)	Bone morphogenetic protein receptors (BMPR1, BMPR1A, BMPR1B, BMPR2), ACVR1, ACVR1B, ACVR1C, ACVR2A, ACVR2B, ACVRL1, Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1, MAP2K2, MAP2K3, MAP2K4, MAP2K5, MAP2K6, MAP2K7

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

RPS6KA1

Contents

Interactions

See also

References

Further reading