RPS6KA1

"HU-1" redirects here. For the helicopter, see UH-1 Iroquois.

RPS6KA1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2WNT, 2Z7Q, 2Z7R, 2Z7S, 3RNY, 4H3P, 4NIF, 5CSJ, 5CSF, 5CSN, 5CSI

Identifiers

Aliases

RPS6KA1, HU-1, MAPKAPK1A, RSK, RSK1, p90Rsk, ribosomal protein S6 kinase A1

External IDs

MGI: 104558 HomoloGene: 55703 GeneCards: RPS6KA1

Gene ontology
Molecular function	• transferase activity • nucleotide binding • protein kinase activity • metal ion binding • cysteine-type endopeptidase inhibitor activity involved in apoptotic process • protein serine/threonine kinase activity • protein binding • protein serine/threonine/tyrosine kinase activity • ATP binding • magnesium ion binding • kinase activity
Cellular component	• cytoplasm • cytosol • nucleoplasm • nucleus
Biological process	• negative regulation of cysteine-type endopeptidase activity involved in apoptotic process • regulation of translation in response to stress • intracellular signal transduction • phosphorylation • negative regulation of apoptotic process • protein phosphorylation • positive regulation of cell growth • hepatocyte proliferation • positive regulation of cell differentiation • positive regulation of hepatic stellate cell activation • cell cycle • regulation of DNA-templated transcription in response to stress • signal transduction • positive regulation of transcription from RNA polymerase II promoter • apoptotic process
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


6195


20111

Ensembl


n/a


ENSMUSG00000003644

UniProt


Q15418


P18653

RefSeq (mRNA)


NM_001006665 NM_002953


NM_001285505 NM_001285506 NM_009097

RefSeq (protein)


NP_001006666.1 NP_002944.2


NP_001272434.1

Location (UCSC)

Chr 1: 26.53 – 26.58 Mb

Chr 4: 133.85 – 133.89 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Ribosomal protein S6 kinase alpha-1 is an enzyme that in humans is encoded by the RPS6KA1 gene.^[3]

Function

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.^[4]

Interactions

RPS6KA1 has been shown to interact with:

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M (Feb 1994). "Human rsk isoforms: cloning and characterization of tissue-specific expression". The American Journal of Physiology. 266 (2 Pt 1): C351–9. PMID 8141249.
↑ "Entrez Gene: RPS6KA1 ribosomal protein S6 kinase, 90kDa, polypeptide 1".
↑ Schouten GJ, Vertegaal AC, Whiteside ST, Israël A, Toebes M, Dorsman JC, van der Eb AJ, Zantema A (Jun 1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase". The EMBO Journal. 16 (11): 3133–44. doi:10.1093/emboj/16.11.3133. PMC 1169932. PMID 9214631.
↑ Roux PP, Richards SA, Blenis J (Jul 2003). "Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity". Molecular and Cellular Biology. 23 (14): 4796–804. doi:10.1128/mcb.23.14.4796-4804.2003. PMC 162206. PMID 12832467.
↑ Eblen ST, Kumar NV, Shah K, Henderson MJ, Watts CK, Shokat KM, Weber MJ (Apr 2003). "Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs". The Journal of Biological Chemistry. 278 (17): 14926–35. doi:10.1074/jbc.M300485200. PMID 12594221.
↑ Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW (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". The Journal of Biological Chemistry. 274 (5): 2893–8. doi:10.1074/jbc.274.5.2893. PMID 9915826.
↑ Suzuki T, Matsuda S, Tsuzuku JK, Yoshida Y, Yamamoto T (Feb 2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob". Genes to Cells. 6 (2): 131–8. doi:10.1046/j.1365-2443.2001.00406.x. PMID 11260258.
↑ Roux PP, Ballif BA, Anjum R, Gygi SP, Blenis J (Sep 2004). "Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase". Proceedings of the National Academy of Sciences of the United States of America. 101 (37): 13489–94. doi:10.1073/pnas.0405659101. PMC 518784. PMID 15342917.
↑ Rolfe M, McLeod LE, Pratt PF, Proud CG (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)". The Biochemical Journal. 388 (Pt 3): 973–84. doi:10.1042/BJ20041888. PMC 1183479. PMID 15757502.
↑ Cavet ME, Lehoux S, Berk BC (May 2003). "14-3-3beta is a p90 ribosomal S6 kinase (RSK) isoform 1-binding protein that negatively regulates RSK kinase activity". The Journal of Biological Chemistry. 278 (20): 18376–83. doi:10.1074/jbc.M208475200. PMID 12618428.

Chen RH, Sarnecki C, Blenis J (Mar 1992). "Nuclear localization and regulation of erk- and rsk-encoded protein kinases". Molecular and Cellular Biology. 12 (3): 915–27. doi:10.1128/mcb.12.3.915. PMC 369523. PMID 1545823.
Tratner I, Ofir R, Verma IM (Mar 1992). "Alteration of a cyclic AMP-dependent protein kinase phosphorylation site in the c-Fos protein augments its transforming potential". Molecular and Cellular Biology. 12 (3): 998–1006. doi:10.1128/mcb.12.3.998. PMC 369532. PMID 1545828.
Maruyama K, Sugano S (Jan 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 (Dec 1993). "Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase". Proceedings of the National Academy of Sciences of the United States of America. 90 (23): 10952–6. doi:10.1073/pnas.90.23.10952. PMC 47899. PMID 8248197.
Rivera VM, Miranti CK, Misra RP, Ginty DD, Chen RH, Blenis J, Greenberg ME (Oct 1993). "A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity". Molecular and Cellular Biology. 13 (10): 6260–73. doi:10.1128/mcb.13.10.6260. PMC 364685. PMID 8413226.
Chen ZJ, Parent L, Maniatis T (Mar 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, Dong F, Löwenberg B, Touw IP (Mar 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 (Jul 1996). "Involvement of p90rsk in neurite outgrowth mediated by the cell adhesion molecule L1". The Journal of Biological Chemistry. 271 (30): 18217–23. doi:10.1074/jbc.271.30.18217. PMID 8663493.
Xing J, Ginty DD, Greenberg ME (Aug 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, Gage FH, Fisher T, Blenis J, Montminy MR (Aug 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 (Nov 1996). "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases". The Journal of Biological Chemistry. 271 (47): 29773–9. doi:10.1074/jbc.271.47.29773. PMID 8939914.
Zaheer A, Lim R (Feb 1997). "Protein kinase A (PKA)- and protein kinase C-phosphorylated glia maturation factor promotes the catalytic activity of PKA". The Journal of Biological Chemistry. 272 (8): 5183–6. doi:10.1074/jbc.272.8.5183. PMID 9030586.
Schouten GJ, Vertegaal AC, Whiteside ST, Israël A, Toebes M, Dorsman JC, van der Eb AJ, Zantema A (Jun 1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase". The EMBO Journal. 16 (11): 3133–44. doi:10.1093/emboj/16.11.3133. PMC 1169932. PMID 9214631.
Li HL, Forman MS, Kurosaki T, Puré E (Jul 1997). "Syk is required for BCR-mediated activation of p90Rsk, but not p70S6k, via a mitogen-activated protein kinase-independent pathway in B cells". The Journal of Biological Chemistry. 272 (29): 18200–8. doi:10.1074/jbc.272.29.18200. PMID 9218456.
Chang YW, Traugh JA (Nov 1997). "Phosphorylation of elongation factor 1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation". The Journal of Biological Chemistry. 272 (45): 28252–7. doi:10.1074/jbc.272.45.28252. PMID 9353277.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 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, Herrera R, Nuñez G (Oct 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, Avruch J, Cohen P (Jan 1998). "Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK". The Journal of Biological Chemistry. 273 (3): 1496–505. doi:10.1074/jbc.273.3.1496. PMID 9430688.
Joel PB, Smith J, Sturgill TW, Fisher TL, Blenis J, Lannigan DA (Apr 1998). "pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167". Molecular and Cellular Biology. 18 (4): 1978–84. doi:10.1128/mcb.18.4.1978. PMC 121427. PMID 9528769.

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) kinase (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

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

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 CDK12 CDC2L5 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

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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RPS6KA1

Function

Interactions

See also

References

Further reading