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{{Infobox_gene}}
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'''Ribosomal protein S6 kinase alpha-2''' is an [[enzyme]] that in humans is encoded by the ''RPS6KA2'' [[gene]].<ref name="pmid8141249">{{cite journal |vauthors=Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M | title = Human rsk isoforms: cloning and characterization of tissue-specific expression | journal = Am J Physiol | volume = 266 | issue = 2 Pt 1 | pages = C351–9 |date=Apr 1994 | pmid = 8141249 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6196| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Ribosomal protein S6 kinase, 90kDa, polypeptide 2
| HGNCid = 10431
| Symbol = RPS6KA2
| AltSymbols =; HU-2; RSK; MAPKAPK1C; RSK3; S6K-alpha; S6K-alpha2; p90-RSK3; pp90RSK3
| OMIM = 601685
| ECnumber = 
| Homologene = 36318
| MGIid = 1342290
| GeneAtlas_image1 = PBB_GE_RPS6KA2_204906_at_tn.png
| GeneAtlas_image2 = PBB_GE_RPS6KA2_212912_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
  | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
  | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6196
    | Hs_Ensembl = ENSG00000071242
    | Hs_RefseqProtein = NP_001006933
    | Hs_RefseqmRNA = NM_001006932
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 166742844
    | Hs_GenLoc_end = 167195791
    | Hs_Uniprot = Q15349
    | Mm_EntrezGene = 20112
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = XM_489703
    | Mm_RefseqProtein = XP_489703
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Ribosomal protein S6 kinase, 90kDa, polypeptide 2''', also known as '''RPS6KA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6196| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6196| accessdate = }}</ref>
| summary_text = This gene encodes a member of the RSK (ribosomal S6 kinase) family of [[serine]] and [[threonine]] [[kinase]]s. 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 [[cellular differentiation|differentiation]]. Alternate transcriptional splice variants, encoding different [[protein isoform|isoforms]], have been characterized.<ref name="entrez" />
}}
}}
==Interactions==
RPS6KA2 has been shown to [[Protein-protein interaction|interact]] with [[MAPK3]]<ref name=pmid12832467>{{cite journal |last=Roux |first=Philippe P |authorlink= |author2=Richards Stephanie A |author3=Blenis John  |date=Jul 2003 |title=Phosphorylation of p90 Ribosomal S6 Kinase (RSK) Regulates Extracellular Signal-Regulated Kinase Docking and RSK Activity |journal=Mol. Cell. Biol. |volume=23 |issue=14 |pages=4796–804 |publisher= |location = United States| issn = 0270-7306| pmid = 12832467 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1128/MCB.23.14.4796-4804.2003 |pmc=162206 }}</ref><ref name=pmid8939914>{{cite journal |last=Zhao |first=Y |authorlink= |author2=Bjorbaek C |author3=Moller D E  |date=Nov 1996 |title=Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases |journal=J. Biol. Chem. |volume=271 |issue=47 |pages=29773–9 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 8939914 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.271.47.29773 }}</ref> and [[MAPK1]].<ref name=pmid12832467/><ref name=pmid8939914/>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi=  }}
*{{cite journal  |vauthors=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi=10.1016/S0163-4453(05)80037-4 }}
*{{cite journal | author=Zhao Y, Bjørbaek C, Weremowicz S, ''et al.'' |title=RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation. |journal=Mol. Cell. Biol. |volume=15 |issue= 8 |pages= 4353-63 |year= 1995 |pmid= 7623830 |doi=  }}
*{{cite journal   |vauthors=Zhao Y, Bjørbaek C, Weremowicz S, etal |title=RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation |journal=Mol. Cell. Biol. |volume=15 |issue= 8 |pages= 4353–63 |year= 1995 |pmid= 7623830 |doi= | pmc=230675 }}
*{{cite journal  | author=Moller DE, Xia CH, Tang W, ''et al.'' |title=Human rsk isoforms: cloning and characterization of tissue-specific expression. |journal=Am. J. Physiol. |volume=266 |issue= 2 Pt 1 |pages= C351-9 |year= 1994 |pmid= 8141249 |doi=  }}
*{{cite journal  |vauthors=Wong EV, Schaefer AW, Landreth G, Lemmon V |title=Involvement of p90rsk in neurite outgrowth mediated by the cell adhesion molecule L1 |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 18217–23 |year= 1996 |pmid= 8663493 |doi=10.1074/jbc.271.30.18217 }}
*{{cite journal  | author=Wong EV, Schaefer AW, Landreth G, Lemmon V |title=Involvement of p90rsk in neurite outgrowth mediated by the cell adhesion molecule L1. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 18217-23 |year= 1996 |pmid= 8663493 |doi=  }}
*{{cite journal  |vauthors=Xing J, Ginty DD, Greenberg ME |title=Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase |journal=Science |volume=273 |issue= 5277 |pages= 959–63 |year= 1996 |pmid= 8688081 |doi=10.1126/science.273.5277.959 |bibcode=1996Sci...273..959X }}
*{{cite journal  | author=Xing J, Ginty DD, Greenberg ME |title=Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. |journal=Science |volume=273 |issue= 5277 |pages= 959-63 |year= 1996 |pmid= 8688081 |doi=  }}
*{{cite journal  |vauthors=Zhao Y, Bjorbaek C, Moller DE |title=Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases |journal=J. Biol. Chem. |volume=271 |issue= 47 |pages= 29773–9 |year= 1997 |pmid= 8939914 |doi=10.1074/jbc.271.47.29773 }}
*{{cite journal  | author=Zhao Y, Bjorbaek C, Moller DE |title=Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases. |journal=J. Biol. Chem. |volume=271 |issue= 47 |pages= 29773-9 |year= 1997 |pmid= 8939914 |doi=  }}
*{{cite journal  |vauthors=Fukunaga R, Hunter T |title=MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates |journal=EMBO J. |volume=16 |issue= 8 |pages= 1921–33 |year= 1997 |pmid= 9155018 |doi= 10.1093/emboj/16.8.1921 | pmc=1169795 }}
*{{cite journal | author=Fukunaga R, Hunter T |title=MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. |journal=EMBO J. |volume=16 |issue= 8 |pages= 1921-33 |year= 1997 |pmid= 9155018 |doi= 10.1093/emboj/16.8.1921 }}
*{{cite journal   |vauthors=del Peso L, González-García M, Page C, etal |title=Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt |journal=Science |volume=278 |issue= 5338 |pages= 687–9 |year= 1997 |pmid= 9381178 |doi=10.1126/science.278.5338.687  }}
*{{cite journal  | author=del Peso L, González-García M, Page C, ''et al.'' |title=Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. |journal=Science |volume=278 |issue= 5338 |pages= 687-9 |year= 1997 |pmid= 9381178 |doi=  }}
*{{cite journal  |vauthors=Deak M, Clifton AD, Lucocq LM, Alessi DR |title=Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB |journal=EMBO J. |volume=17 |issue= 15 |pages= 4426–41 |year= 1998 |pmid= 9687510 |doi= 10.1093/emboj/17.15.4426 | pmc=1170775 }}
*{{cite journal  | author=Deak M, Clifton AD, Lucocq LM, Alessi DR |title=Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. |journal=EMBO J. |volume=17 |issue= 15 |pages= 4426-41 |year= 1998 |pmid= 9687510 |doi= 10.1093/emboj/17.15.4426 }}
*{{cite journal  |vauthors=Du K, Montminy M |title=CREB is a regulatory target for the protein kinase Akt/PKB |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32377–9 |year= 1999 |pmid= 9829964 |doi=10.1074/jbc.273.49.32377  }}
*{{cite journal  | author=Du K, Montminy M |title=CREB is a regulatory target for the protein kinase Akt/PKB. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32377-9 |year= 1999 |pmid= 9829964 |doi=  }}
*{{cite journal  |vauthors=Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW |title=Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo |journal=J. Biol. Chem. |volume=274 |issue= 5 |pages= 2893–8 |year= 1999 |pmid= 9915826 |doi=10.1074/jbc.274.5.2893 }}
*{{cite journal | author=Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW |title=Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo. |journal=J. Biol. Chem. |volume=274 |issue= 5 |pages= 2893-8 |year= 1999 |pmid= 9915826 |doi=  }}
*{{cite journal   |vauthors=Jensen CJ, Buch MB, Krag TO, etal |title=90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1 |journal=J. Biol. Chem. |volume=274 |issue= 38 |pages= 27168–76 |year= 1999 |pmid= 10480933 |doi=10.1074/jbc.274.38.27168 }}
*{{cite journal  | author=Jensen CJ, Buch MB, Krag TO, ''et al.'' |title=90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1. |journal=J. Biol. Chem. |volume=274 |issue= 38 |pages= 27168-76 |year= 1999 |pmid= 10480933 |doi=  }}
*{{cite journal  | author=Schimenti JC |title=ORFless, intronless, and mutant transcription units in the mouse t complex responder (Tcr) locus |journal=Mamm. Genome |volume=10 |issue= 10 |pages= 969–76 |year= 2000 |pmid= 10501965 |doi=10.1007/s003359901142 }}
*{{cite journal  | author=Schimenti JC |title=ORFless, intronless, and mutant transcription units in the mouse t complex responder (Tcr) locus. |journal=Mamm. Genome |volume=10 |issue= 10 |pages= 969-76 |year= 2000 |pmid= 10501965 |doi=  }}
*{{cite journal  |vauthors=Scheid MP, Schubert KM, Duronio V |title=Regulation of bad phosphorylation and association with Bcl-x(L) by the MAPK/Erk kinase |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 31108–13 |year= 1999 |pmid= 10521512 |doi=10.1074/jbc.274.43.31108 }}
*{{cite journal  | author=Scheid MP, Schubert KM, Duronio V |title=Regulation of bad phosphorylation and association with Bcl-x(L) by the MAPK/Erk kinase. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 31108-13 |year= 1999 |pmid= 10521512 |doi= }}
*{{cite journal  |vauthors=Tan Y, Demeter MR, Ruan H, Comb MJ |title=BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25865–9 |year= 2000 |pmid= 10837486 |doi= 10.1074/jbc.M004199200 }}
*{{cite journal  | author=Tan Y, Demeter MR, Ruan H, Comb MJ |title=BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25865-9 |year= 2000 |pmid= 10837486 |doi= 10.1074/jbc.M004199200 }}
*{{cite journal  |vauthors=Lizcano JM, Morrice N, Cohen P |title=Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155 |journal=Biochem. J. |volume=349 |issue= Pt 2 |pages= 547–57 |year= 2001 |pmid= 10880354 |doi=10.1042/0264-6021:3490547  | pmc=1221178  }}
*{{cite journal | author=Lizcano JM, Morrice N, Cohen P |title=Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155. |journal=Biochem. J. |volume=349 |issue= Pt 2 |pages= 547-57 |year= 2001 |pmid= 10880354 |doi=  }}
*{{cite journal   |vauthors=Datta SR, Katsov A, Hu L, etal |title=14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation |journal=Mol. Cell |volume=6 |issue= 1 |pages= 41–51 |year= 2000 |pmid= 10949026 |doi=10.1016/S1097-2765(00)00006-X }}
*{{cite journal | author=Datta SR, Katsov A, Hu L, ''et al.'' |title=14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation. |journal=Mol. Cell |volume=6 |issue= 1 |pages= 41-51 |year= 2000 |pmid= 10949026 |doi= }}
*{{cite journal   |vauthors=Gudi T, Casteel DE, Vinson C, etal |title=NO activation of fos promoter elements requires nuclear translocation of G-kinase I and CREB phosphorylation but is independent of MAP kinase activation |journal=Oncogene |volume=19 |issue= 54 |pages= 6324–33 |year= 2001 |pmid= 11175347 |doi= 10.1038/sj.onc.1204007 }}
*{{cite journal  | author=Gudi T, Casteel DE, Vinson C, ''et al.'' |title=NO activation of fos promoter elements requires nuclear translocation of G-kinase I and CREB phosphorylation but is independent of MAP kinase activation. |journal=Oncogene |volume=19 |issue= 54 |pages= 6324-33 |year= 2001 |pmid= 11175347 |doi= 10.1038/sj.onc.1204007 }}
*{{cite journal  |vauthors=Willard FS, Crouch MF |title=MEK, ERK, and p90RSK are present on mitotic tubulin in Swiss 3T3 cells: a role for the MAP kinase pathway in regulating mitotic exit |journal=Cell. Signal. |volume=13 |issue= 9 |pages= 653–64 |year= 2001 |pmid= 11495723 |doi=10.1016/S0898-6568(01)00185-1 }}
*{{cite journal  | author=Willard FS, Crouch MF |title=MEK, ERK, and p90RSK are present on mitotic tubulin in Swiss 3T3 cells: a role for the MAP kinase pathway in regulating mitotic exit. |journal=Cell. Signal. |volume=13 |issue= 9 |pages= 653-64 |year= 2001 |pmid= 11495723 |doi= }}
*{{cite journal   |vauthors=Schinelli S, Zanassi P, Paolillo M, etal |title=Stimulation of endothelin B receptors in astrocytes induces cAMP response element-binding protein phosphorylation and c-fos expression via multiple mitogen-activated protein kinase signaling pathways |journal=J. Neurosci. |volume=21 |issue= 22 |pages= 8842–53 |year= 2001 |pmid= 11698596 |doi=  }}
*{{cite journal | author=Schinelli S, Zanassi P, Paolillo M, ''et al.'' |title=Stimulation of endothelin B receptors in astrocytes induces cAMP response element-binding protein phosphorylation and c-fos expression via multiple mitogen-activated protein kinase signaling pathways. |journal=J. Neurosci. |volume=21 |issue= 22 |pages= 8842-53 |year= 2001 |pmid= 11698596 |doi=  }}
}}
}}
{{refend}}
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{{protein-stub}}
{{Serine/threonine-specific protein kinases}}
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Latest revision as of 01:48, 26 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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View/Edit Human

Ribosomal protein S6 kinase alpha-2 is an enzyme that in humans is encoded by the RPS6KA2 gene.[1][2]

This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine and 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. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[2]

Interactions

RPS6KA2 has been shown to interact with MAPK3[3][4] and MAPK1.[3][4]

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2".
  3. ↑ 3.0 3.1 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.
  4. ↑ 4.0 4.1 Zhao, Y; Bjorbaek C; Moller D E (Nov 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.

Further reading


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