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Ribosomal protein S6 kinase beta-1 (S6K-beta-1) (S6K1) (EC 2.7.11.1) (70 kDa ribosomal protein S6 kinase 1) (P70S6K1) (p70-S6K 1) (Ribosomal protein S6 kinase I) (Serine/threonine-protein kinase 14A) (p70 ribosomal S6 kinase alpha) (p70 S6 kinase alpha) (p70 S6K-alpha) (p70 S6KA)

 KS6B1_HUMAN             Reviewed;         525 AA.
P23443; B2R779; B4DLT4; B4DTG1; E7ESB8; F6UYM1; Q7Z721;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 2.
13-FEB-2019, entry version 199.
RecName: Full=Ribosomal protein S6 kinase beta-1;
Short=S6K-beta-1;
Short=S6K1;
EC=2.7.11.1 {ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:18952604, ECO:0000269|PubMed:19085255, ECO:0000269|PubMed:28178239};
AltName: Full=70 kDa ribosomal protein S6 kinase 1;
Short=P70S6K1;
Short=p70-S6K 1;
AltName: Full=Ribosomal protein S6 kinase I;
AltName: Full=Serine/threonine-protein kinase 14A;
AltName: Full=p70 ribosomal S6 kinase alpha;
Short=p70 S6 kinase alpha;
Short=p70 S6K-alpha;
Short=p70 S6KA;
Name=RPS6KB1; Synonyms=STK14A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA I AND ALPHA II), AND
ALTERNATIVE INITIATION.
PubMed=1922062; DOI=10.1128/MCB.11.11.5541;
Grove J., Bonerjee P., Balasubramanyam A., Coffer P., Price D.J.,
Avruch J., Woodgett J.R.;
"Cloning and expression of two human p70 S6 kinase polypeptides
differing only at their amino termini.";
Mol. Cell. Biol. 11:5541-5550(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA I; 2 AND 4).
TISSUE=Placenta, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY.
PubMed=9804755; DOI=10.1074/jbc.273.46.30061;
Gout I., Minami T., Hara K., Tsujishita Y., Filonenko V.,
Waterfield M.D., Yonezawa K.;
"Molecular cloning and characterization of a novel p70 S6 kinase, p70
S6 kinase beta containing a proline-rich region.";
J. Biol. Chem. 273:30061-30064(1998).
[7]
ACTIVITY REGULATION, PHOSPHORYLATION AT THR-252, AND MUTAGENESIS OF
THR-412; SER-434; SER-441; THR-444 AND SER-447.
PubMed=9445476; DOI=10.1126/science.279.5351.707;
Pullen N., Dennis P.B., Andjelkovic M., Dufner A., Kozma S.C.,
Hemmings B.A., Thomas G.;
"Phosphorylation and activation of p70s6k by PDK1.";
Science 279:707-710(1998).
[8]
FUNCTION IN PHOSPHORYLATION OF EEF2K, AND FUNCTION IN TRANSLATION
REGULATION.
PubMed=11500364; DOI=10.1093/emboj/20.16.4370;
Wang X., Li W., Williams M., Terada N., Alessi D.R., Proud C.G.;
"Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6
kinase.";
EMBO J. 20:4370-4379(2001).
[9]
INTERACTION WITH RPTOR.
PubMed=12150926; DOI=10.1016/S0092-8674(02)00833-4;
Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S.,
Tokunaga C., Avruch J., Yonezawa K.;
"Raptor, a binding partner of target of rapamycin (TOR), mediates TOR
action.";
Cell 110:177-189(2002).
[10]
FUNCTION, AND INTERACTION WITH TRAF4.
PubMed=12801526; DOI=10.1016/S0145-2126(02)00325-9;
Fleckenstein D.S., Dirks W.G., Drexler H.G., Quentmeier H.;
"Tumor necrosis factor receptor-associated factor (TRAF) 4 is a new
binding partner for the p70S6 serine/threonine kinase.";
Leuk. Res. 27:687-694(2003).
[11]
FUNCTION, AND INTERACTION WITH POLDIP3.
PubMed=15341740; DOI=10.1016/j.cub.2004.08.061;
Richardson C.J., Broenstrup M., Fingar D.C., Julich K., Ballif B.A.,
Gygi S., Blenis J.;
"SKAR is a specific target of S6 kinase 1 in cell growth control.";
Curr. Biol. 14:1540-1549(2004).
[12]
FUNCTION IN PHOSPHORYLATION OF EIF4B.
PubMed=15071500; DOI=10.1038/sj.emboj.7600193;
Raught B., Peiretti F., Gingras A.C., Livingstone M., Shahbazian D.,
Mayeur G.L., Polakiewicz R.D., Sonenberg N., Hershey J.W.;
"Phosphorylation of eucaryotic translation initiation factor 4B Ser422
is modulated by S6 kinases.";
EMBO J. 23:1761-1769(2004).
[13]
FUNCTION IN CELL CYCLE PROGRESSION.
PubMed=14673156; DOI=10.1128/MCB.24.1.200-216.2004;
Fingar D.C., Richardson C.J., Tee A.R., Cheatham L., Tsou C.,
Blenis J.;
"mTOR controls cell cycle progression through its cell growth
effectors S6K1 and 4E-BP1/eukaryotic translation initiation factor
4E.";
Mol. Cell. Biol. 24:200-216(2004).
[14]
FUNCTION IN TRANSLATION INITIATION, INTERACTION WITH EIF3B AND EIF3C,
AND MUTAGENESIS OF THR-412.
PubMed=16286006; DOI=10.1016/j.cell.2005.10.024;
Holz M.K., Ballif B.A., Gygi S.P., Blenis J.;
"mTOR and S6K1 mediate assembly of the translation preinitiation
complex through dynamic protein interchange and ordered
phosphorylation events.";
Cell 123:569-580(2005).
[15]
FUNCTION IN PHOSPHORYLATION OF GSK3B.
PubMed=17052453; DOI=10.1016/j.molcel.2006.09.019;
Zhang H.H., Lipovsky A.I., Dibble C.C., Sahin M., Manning B.D.;
"S6K1 regulates GSK3 under conditions of mTOR-dependent feedback
inhibition of Akt.";
Mol. Cell 24:185-197(2006).
[16]
FUNCTION.
PubMed=17053147; DOI=10.1126/science.1130276;
Dorrello N.V., Peschiaroli A., Guardavaccaro D., Colburn N.H.,
Sherman N.E., Pagano M.;
"S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein
translation and cell growth.";
Science 314:467-471(2006).
[17]
ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-167 AND SER-394.
PubMed=17446865; DOI=10.1038/sj.emboj.7601682;
Hauge C., Antal T.L., Hirschberg D., Doehn U., Thorup K.,
Idrissova L., Hansen K., Jensen O.N., Jorgensen T.J., Biondi R.M.,
Frodin M.;
"Mechanism for activation of the growth factor-activated AGC kinases
by turn motif phosphorylation.";
EMBO J. 26:2251-2261(2007).
[18]
FUNCTION IN PHOSPHORYLATION OF URI1, CATALYTIC ACTIVITY,
DEPHOSPHORYLATION AT THR-412 BY PPP1CC, AND SUBCELLULAR LOCATION.
PubMed=17936702; DOI=10.1016/j.molcel.2007.08.010;
Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M.,
Aebersold R., Hess D., Krek W.;
"S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes
activates a negative feedback program that counters S6K1 survival
signaling.";
Mol. Cell 28:28-40(2007).
[19]
PHOSPHORYLATION AT THR-412.
PubMed=18925875; DOI=10.1042/BJ20081668;
Garcia-Martinez J.M., Alessi D.R.;
"mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation
and activation of serum- and glucocorticoid-induced protein kinase 1
(SGK1).";
Biochem. J. 416:375-385(2008).
[20]
FUNCTION IN PHOSPHORYLATION OF IRS1, CATALYTIC ACTIVITY, FUNCTION IN
GLUCOSE HOMEOSTASIS, AND INTERACTION WITH IRS1.
PubMed=18952604; DOI=10.1074/jbc.M806480200;
Zhang J., Gao Z., Yin J., Quon M.J., Ye J.;
"S6K directly phosphorylates IRS-1 on Ser-270 to promote insulin
resistance in response to TNF-(alpha) signaling through IKK2.";
J. Biol. Chem. 283:35375-35382(2008).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
FUNCTION, CATALYTIC ACTIVITY, ALTERNATIVE SPLICING, PHOSPHORYLATION AT
SER-394; THR-412; THR-444 AND SER-447, AND SUBCELLULAR LOCATION.
PubMed=19085255; DOI=10.1080/08977190802556986;
Kim D., Akcakanat A., Singh G., Sharma C., Meric-Bernstam F.;
"Regulation and localization of ribosomal protein S6 kinase 1
isoforms.";
Growth Factors 27:12-21(2009).
[23]
ACTIVITY REGULATION, AND MUTAGENESIS OF THR-412.
PubMed=19570988; DOI=10.1074/jbc.M109.032177;
Keshwani M.M., Gao X., Harris T.K.;
"Mechanism of PDK1-catalyzed Thr-229 phosphorylation of the S6K1
protein kinase.";
J. Biol. Chem. 284:22611-22624(2009).
[24]
FUNCTION IN PHOSPHORYLATION OF RICTOR.
PubMed=19720745; DOI=10.1128/MCB.00735-09;
Dibble C.C., Asara J.M., Manning B.D.;
"Characterization of Rictor phosphorylation sites reveals direct
regulation of mTOR complex 2 by S6K1.";
Mol. Cell. Biol. 29:5657-5670(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[26]
FUNCTION IN PHOSPHORYLATION OF RICTOR.
PubMed=19995915; DOI=10.1128/MCB.00601-09;
Julien L.A., Carriere A., Moreau J., Roux P.P.;
"mTORC1-activated S6K1 phosphorylates Rictor on threonine 1135 and
regulates mTORC2 signaling.";
Mol. Cell. Biol. 30:908-921(2010).
[27]
FUNCTION IN PHOSPHORYLATION OF RICTOR.
PubMed=19935711; DOI=10.1038/onc.2009.401;
Treins C., Warne P.H., Magnuson M.A., Pende M., Downward J.;
"Rictor is a novel target of p70 S6 kinase-1.";
Oncogene 29:1003-1016(2010).
[28]
REVIEW ON FUNCTION, AND REVIEW ON ACTIVITY REGULATION.
PubMed=18092230; DOI=10.1080/08977190701779101;
Jastrzebski K., Hannan K.M., Tchoubrieva E.B., Hannan R.D.,
Pearson R.B.;
"Coordinate regulation of ribosome biogenesis and function by the
ribosomal protein S6 kinase, a key mediator of mTOR function.";
Growth Factors 25:209-226(2007).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; THR-444; SER-447
AND SER-452, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
REVIEW ON FUNCTION, AND REVIEW ON ACTIVITY REGULATION.
PubMed=20932932; DOI=10.1016/j.biocel.2010.09.018;
Fenton T.R., Gout I.T.;
"Functions and regulation of the 70kDa ribosomal S6 kinases.";
Int. J. Biochem. Cell Biol. 43:47-59(2011).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-444 AND SER-447, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
FUNCTION, PHOSPHORYLATION OF CAD, AND PHOSPHORYLATION BY MTOR.
PubMed=23429703; DOI=10.1126/science.1228792;
Ben-Sahra I., Howell J.J., Asara J.M., Manning B.D.;
"Stimulation of de novo pyrimidine synthesis by growth signaling
through mTOR and S6K1.";
Science 339:1323-1328(2013).
[33]
INTERACTION WITH IER5.
PubMed=26496226; DOI=10.1016/j.febslet.2015.10.013;
Kawabata S., Ishita Y., Ishikawa Y., Sakurai H.;
"Immediate-early response 5 (IER5) interacts with protein phosphatase
2A and regulates the phosphorylation of ribosomal protein S6 kinase
and heat shock factor 1.";
FEBS Lett. 589:3679-3685(2015).
[34]
FUNCTION IN PHOSPHORYLATION OF EPRS, CATALYTIC ACTIVITY, AND ACTIVITY
REGULATION.
PubMed=28178239; DOI=10.1038/nature21380;
Arif A., Terenzi F., Potdar A.A., Jia J., Sacks J., China A.,
Halawani D., Vasu K., Li X., Brown J.M., Chen J., Kozma S.C.,
Thomas G., Fox P.L.;
"EPRS is a critical mTORC1-S6K1 effector that influences adiposity in
mice.";
Nature 542:357-361(2017).
[35]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 75-399, AND PHOSPHORYLATION
AT THR-252.
PubMed=19864428; DOI=10.1074/jbc.M109.040667;
Sunami T., Byrne N., Diehl R.E., Funabashi K., Hall D.L., Ikuta M.,
Patel S.B., Shipman J.M., Smith R.F., Takahashi I., Zugay-Murphy J.,
Iwasawa Y., Lumb K.J., Munshi S.K., Sharma S.;
"Structural basis of human p70 ribosomal S6 kinase-1 regulation by
activation loop phosphorylation.";
J. Biol. Chem. 285:4587-4594(2010).
[36]
VARIANT [LARGE SCALE ANALYSIS] GLU-289.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[37]
VARIANTS [LARGE SCALE ANALYSIS] ILE-225; CYS-272; CYS-276 AND ALA-398.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Serine/threonine-protein kinase that acts downstream of
mTOR signaling in response to growth factors and nutrients to
promote cell proliferation, cell growth and cell cycle
progression. Regulates protein synthesis through phosphorylation
of EIF4B, RPS6 and EEF2K, and contributes to cell survival by
repressing the pro-apoptotic function of BAD. Under conditions of
nutrient depletion, the inactive form associates with the EIF3
translation initiation complex. Upon mitogenic stimulation,
phosphorylation by the mammalian target of rapamycin complex 1
(mTORC1) leads to dissociation from the EIF3 complex and
activation. The active form then phosphorylates and activates
several substrates in the pre-initiation complex, including the
EIF2B complex and the cap-binding complex component EIF4B. Also
controls translation initiation by phosphorylating a negative
regulator of EIF4A, PDCD4, targeting it for ubiquitination and
subsequent proteolysis. Promotes initiation of the pioneer round
of protein synthesis by phosphorylating POLDIP3/SKAR. In response
to IGF1, activates translation elongation by phosphorylating EEF2
kinase (EEF2K), which leads to its inhibition and thus activation
of EEF2. Also plays a role in feedback regulation of mTORC2 by
mTORC1 by phosphorylating RICTOR, resulting in the inhibition of
mTORC2 and AKT1 signaling. Mediates cell survival by
phosphorylating the pro-apoptotic protein BAD and suppressing its
pro-apoptotic function. Phosphorylates mitochondrial URI1 leading
to dissociation of a URI1-PPP1CC complex. The free mitochondrial
PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is
proposed to be a negative feedback mechanism for the RPS6KB1 anti-
apoptotic function. Mediates TNF-alpha-induced insulin resistance
by phosphorylating IRS1 at multiple serine residues, resulting in
accelerated degradation of IRS1. In cells lacking functional TSC1-
2 complex, constitutively phosphorylates and inhibits GSK3B. May
be involved in cytoskeletal rearrangement through binding to
neurabin. Phosphorylates and activates the pyrimidine biosynthesis
enzyme CAD, downstream of MTOR (PubMed:11500364, PubMed:12801526,
PubMed:14673156, PubMed:15071500, PubMed:15341740,
PubMed:16286006, PubMed:17052453, PubMed:17053147,
PubMed:17936702, PubMed:18952604, PubMed:19085255,
PubMed:19720745, PubMed:19935711, PubMed:19995915,
PubMed:23429703). Following activation by mTORC1, phosphorylates
EPRS and thereby plays a key role in fatty acid uptake by
adipocytes and also most probably in interferon-gamma-induced
translation inhibition (PubMed:28178239).
{ECO:0000269|PubMed:11500364, ECO:0000269|PubMed:12801526,
ECO:0000269|PubMed:14673156, ECO:0000269|PubMed:15071500,
ECO:0000269|PubMed:15341740, ECO:0000269|PubMed:16286006,
ECO:0000269|PubMed:17052453, ECO:0000269|PubMed:17053147,
ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:18952604,
ECO:0000269|PubMed:19085255, ECO:0000269|PubMed:19720745,
ECO:0000269|PubMed:19935711, ECO:0000269|PubMed:19995915,
ECO:0000269|PubMed:23429703, ECO:0000269|PubMed:28178239}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000269|PubMed:17936702,
ECO:0000269|PubMed:18952604, ECO:0000269|PubMed:19085255,
ECO:0000269|PubMed:28178239};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000269|PubMed:17936702,
ECO:0000269|PubMed:18952604, ECO:0000269|PubMed:19085255,
ECO:0000269|PubMed:28178239};
-!- ACTIVITY REGULATION: Activation requires multiple phosphorylation
events on serine/threonine residues. Activation appears to be
first mediated by phosphorylation of multiple sites in the
autoinhibitory domain, which facilitates phosphorylation at Thr-
412, disrupting the autoinhibitory mechanism and allowing
phosphorylation of Thr-252 by PDPK1. The active conformation of
the kinase is believed to be stabilized by a mechanism involving
three conserved phosphorylation sites located in the kinase domain
activation loop (Thr-252) and in the AGC-kinase C-terminal domain
(Ser-394 in the middle of the tail/linker region and Thr-412
within a hydrophobic motif at its end). Activated by mTORC1;
isoform Alpha I and isoform Alpha II are sensitive to rapamycin,
which inhibits activating phosphorylation at Thr-412. Activated by
PDPK1. {ECO:0000269|PubMed:17446865, ECO:0000269|PubMed:19570988,
ECO:0000269|PubMed:28178239, ECO:0000269|PubMed:9445476}.
-!- SUBUNIT: Interacts with PPP1R9A/neurabin-1 (By similarity).
Interacts with RPTOR (PubMed:12150926). Interacts with IRS1
(PubMed:18952604). Interacts with EIF3B and EIF3C
(PubMed:16286006). Interacts with TRAF4 (PubMed:12801526).
Interacts with POLDIP3 (PubMed:15341740). Interacts (via N-
terminus) with IER5 (PubMed:26496226).
{ECO:0000250|UniProtKB:P67999, ECO:0000269|PubMed:12150926,
ECO:0000269|PubMed:12801526, ECO:0000269|PubMed:15341740,
ECO:0000269|PubMed:16286006, ECO:0000269|PubMed:18952604,
ECO:0000269|PubMed:26496226}.
-!- INTERACTION:
P31749:AKT1; NbExp=2; IntAct=EBI-1775921, EBI-296087;
P55884:EIF3B; NbExp=3; IntAct=EBI-1775921, EBI-366696;
P08151:GLI1; NbExp=4; IntAct=EBI-1775921, EBI-308084;
Q5VY09:IER5; NbExp=2; IntAct=EBI-1775921, EBI-1774000;
Q00005:PPP2R2B; NbExp=2; IntAct=EBI-1775921, EBI-1052159;
-!- SUBCELLULAR LOCATION: Cell junction, synapse, synaptosome
{ECO:0000250}. Mitochondrion outer membrane. Mitochondrion.
Note=Colocalizes with URI1 at mitochondrion.
-!- SUBCELLULAR LOCATION: Isoform Alpha I: Nucleus. Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform Alpha II: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=Alpha I; Synonyms=p80-S6K 1;
IsoId=P23443-1; Sequence=Displayed;
Name=Alpha II;
IsoId=P23443-2; Sequence=VSP_018839;
Name=2;
IsoId=P23443-3; Sequence=VSP_054613;
Note=No experimental confirmation available.;
Name=4;
IsoId=P23443-5; Sequence=VSP_055026;
Name=3;
IsoId=P23443-4; Sequence=VSP_054614;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:9804755}.
-!- DOMAIN: The autoinhibitory domain is believed to block
phosphorylation within the AGC-kinase C-terminal domain and the
activation loop.
-!- DOMAIN: The TOS (TOR signaling) motif is essential for activation
by mTORC1. {ECO:0000250}.
-!- PTM: Phosphorylation at Thr-412 is regulated by mTORC1. The
phosphorylation at this site is maintained by an agonist-dependent
autophosphorylation mechanism (By similarity). Activated by
phosphorylation at Thr-252 by PDPK1. Dephosphorylation by PPP1CC
at Thr-412 in mitochondrion. {ECO:0000250,
ECO:0000269|PubMed:18925875, ECO:0000269|PubMed:19085255,
ECO:0000269|PubMed:19864428, ECO:0000269|PubMed:23429703,
ECO:0000269|PubMed:9445476}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. S6 kinase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M60724; AAA36410.1; -; mRNA.
EMBL; M60725; AAA36411.1; -; mRNA.
EMBL; AK297147; BAG59646.1; -; mRNA.
EMBL; AK300202; BAG61973.1; -; mRNA.
EMBL; AK312875; BAG35726.1; -; mRNA.
EMBL; AC004686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94384.1; -; Genomic_DNA.
EMBL; BC053365; AAH53365.1; -; mRNA.
CCDS; CCDS11621.1; -. [P23443-1]
CCDS; CCDS62271.1; -. [P23443-4]
CCDS; CCDS62272.1; -. [P23443-5]
CCDS; CCDS62273.1; -. [P23443-3]
PIR; A41687; A41687.
RefSeq; NP_001258971.1; NM_001272042.1. [P23443-5]
RefSeq; NP_001258972.1; NM_001272043.1. [P23443-4]
RefSeq; NP_001258973.1; NM_001272044.1. [P23443-3]
RefSeq; NP_001258989.1; NM_001272060.1. [P23443-2]
RefSeq; NP_003152.1; NM_003161.3. [P23443-1]
UniGene; Hs.463642; -.
PDB; 3A60; X-ray; 2.80 A; A/B=75-399.
PDB; 3A61; X-ray; 3.43 A; A=75-399.
PDB; 3A62; X-ray; 2.35 A; A=75-399.
PDB; 3WE4; X-ray; 2.00 A; A=78-399.
PDB; 3WF5; X-ray; 2.10 A; A=78-399.
PDB; 3WF6; X-ray; 2.03 A; A=78-399.
PDB; 3WF7; X-ray; 1.85 A; A=78-399.
PDB; 3WF8; X-ray; 1.98 A; A=78-399.
PDB; 3WF9; X-ray; 2.04 A; A=78-399.
PDB; 4L3J; X-ray; 2.10 A; A=75-375.
PDB; 4L3L; X-ray; 2.10 A; A=75-375.
PDB; 4L42; X-ray; 2.80 A; A=75-417.
PDB; 4L43; X-ray; 3.00 A; A=75-417.
PDB; 4L44; X-ray; 2.90 A; A=75-417.
PDB; 4L45; X-ray; 2.90 A; A=75-417.
PDB; 4L46; X-ray; 3.01 A; A=75-417.
PDB; 4RLO; X-ray; 2.53 A; A/B=85-372.
PDB; 4RLP; X-ray; 2.79 A; A=85-372.
PDB; 5WBH; X-ray; 1.75 A; W=412-437.
PDB; 5WBK; X-ray; 3.11 A; T=24-37.
PDBsum; 3A60; -.
PDBsum; 3A61; -.
PDBsum; 3A62; -.
PDBsum; 3WE4; -.
PDBsum; 3WF5; -.
PDBsum; 3WF6; -.
PDBsum; 3WF7; -.
PDBsum; 3WF8; -.
PDBsum; 3WF9; -.
PDBsum; 4L3J; -.
PDBsum; 4L3L; -.
PDBsum; 4L42; -.
PDBsum; 4L43; -.
PDBsum; 4L44; -.
PDBsum; 4L45; -.
PDBsum; 4L46; -.
PDBsum; 4RLO; -.
PDBsum; 4RLP; -.
PDBsum; 5WBH; -.
PDBsum; 5WBK; -.
ProteinModelPortal; P23443; -.
SMR; P23443; -.
BioGrid; 112112; 71.
DIP; DIP-29986N; -.
ELM; P23443; -.
IntAct; P23443; 29.
MINT; P23443; -.
STRING; 9606.ENSP00000225577; -.
BindingDB; P23443; -.
ChEMBL; CHEMBL4501; -.
GuidetoPHARMACOLOGY; 1525; -.
iPTMnet; P23443; -.
PhosphoSitePlus; P23443; -.
BioMuta; RPS6KB1; -.
DMDM; 54041234; -.
EPD; P23443; -.
jPOST; P23443; -.
MaxQB; P23443; -.
PaxDb; P23443; -.
PeptideAtlas; P23443; -.
PRIDE; P23443; -.
ProteomicsDB; 54095; -.
ProteomicsDB; 54096; -. [P23443-2]
DNASU; 6198; -.
Ensembl; ENST00000225577; ENSP00000225577; ENSG00000108443. [P23443-1]
Ensembl; ENST00000393021; ENSP00000376744; ENSG00000108443. [P23443-3]
Ensembl; ENST00000406116; ENSP00000384335; ENSG00000108443. [P23443-4]
Ensembl; ENST00000443572; ENSP00000441993; ENSG00000108443. [P23443-5]
GeneID; 6198; -.
KEGG; hsa:6198; -.
UCSC; uc002ixy.5; human. [P23443-1]
CTD; 6198; -.
DisGeNET; 6198; -.
EuPathDB; HostDB:ENSG00000108443.13; -.
GeneCards; RPS6KB1; -.
HGNC; HGNC:10436; RPS6KB1.
HPA; CAB003838; -.
HPA; CAB018346; -.
HPA; HPA039442; -.
MIM; 608938; gene.
neXtProt; NX_P23443; -.
OpenTargets; ENSG00000108443; -.
PharmGKB; PA34851; -.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00940000154203; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; P23443; -.
KO; K04688; -.
OMA; RSPRKFP; -.
OrthoDB; 1132245at2759; -.
PhylomeDB; P23443; -.
TreeFam; TF313438; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-166208; mTORC1-mediated signalling.
SABIO-RK; P23443; -.
SignaLink; P23443; -.
SIGNOR; P23443; -.
ChiTaRS; RPS6KB1; human.
EvolutionaryTrace; P23443; -.
GeneWiki; P70-S6_Kinase_1; -.
GenomeRNAi; 6198; -.
PRO; PR:P23443; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108443; Expressed in 211 organ(s), highest expression level in cerebellar vermis.
ExpressionAtlas; P23443; baseline and differential.
Genevisible; P23443; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
GO; GO:0042277; F:peptide binding; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:MGI.
GO; GO:0004711; F:ribosomal protein S6 kinase activity; IBA:GO_Central.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0016477; P:cell migration; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0007281; P:germ cell development; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0044539; P:long-chain fatty acid import into cell; ISS:UniProtKB.
GO; GO:0007616; P:long-term memory; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; IEA:Ensembl.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
GO; GO:0045948; P:positive regulation of translational initiation; IMP:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
GO; GO:0046324; P:regulation of glucose import; IEA:Ensembl.
GO; GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0009408; P:response to heat; IEA:Ensembl.
GO; GO:0043201; P:response to leucine; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0009611; P:response to wounding; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0014732; P:skeletal muscle atrophy; IEA:Ensembl.
GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
GO; GO:0031929; P:TOR signaling; IDA:UniProtKB.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR016238; Ribosomal_S6_kinase.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000605; Ribsml_S6_kin_1; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative initiation;
Alternative splicing; Apoptosis; ATP-binding; Cell cycle;
Cell junction; Complete proteome; Cytoplasm; Kinase; Membrane;
Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Synapse; Synaptosome; Transferase;
Translation regulation.
CHAIN 1 525 Ribosomal protein S6 kinase beta-1.
/FTId=PRO_0000024342.
DOMAIN 91 352 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 353 423 AGC-kinase C-terminal.
NP_BIND 97 105 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 424 525 Autoinhibitory domain.
MOTIF 28 32 TOS motif.
ACT_SITE 218 218 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 123 123 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 252 252 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:19864428,
ECO:0000269|PubMed:9445476}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000269|PubMed:19085255}.
MOD_RES 412 412 Phosphothreonine; by MTOR, NEK6 and NEK7.
{ECO:0000250|UniProtKB:P67999}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:P67999}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 444 444 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19085255}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19085255}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 516 516 N6-acetyllysine.
{ECO:0000250|UniProtKB:P67999}.
VAR_SEQ 1 53 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054613.
VAR_SEQ 1 23 Missing (in isoform Alpha II).
{ECO:0000303|PubMed:1922062}.
/FTId=VSP_018839.
VAR_SEQ 104 126 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055026.
VAR_SEQ 448 525 PVKFSPGDFWGRGASASTANPQTPVEYPMETSGIEQMDVTM
SGEASAPLPIRQPNSGPYKKQAFPMISKRPEHLRMNL ->
TAMC (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054614.
VARIANT 225 225 M -> I. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040639.
VARIANT 272 272 R -> C (in dbSNP:rs766645749).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040640.
VARIANT 276 276 W -> C. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040641.
VARIANT 289 289 G -> E (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035628.
VARIANT 398 398 S -> A. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040642.
MUTAGEN 167 167 K->N: Greatly reduces activity. Greatly
reduces phosphorylation at T-412 and
moderately reduces phosphorylation at T-
252. {ECO:0000269|PubMed:17446865}.
MUTAGEN 394 394 S->A: Loss of activity. Loss of
phosphorylation at T-412.
{ECO:0000269|PubMed:17446865}.
MUTAGEN 412 412 T->E: Mimics phosphorylation. Facilitates
phosphorylation of T-252 by PDPK1; when
associated with E-434; E-441; E-444 and
E-447. Mimics phosphorylation. No effect
on interaction with PDPK1 and
phosphorylation of T-252. Impairs
association with the eIF3 complex.
{ECO:0000269|PubMed:16286006,
ECO:0000269|PubMed:19570988,
ECO:0000269|PubMed:9445476}.
MUTAGEN 434 434 S->E: Facilitates phosphorylation of T-
252 by PDPK1; when associated with E-412;
E-441; E-444 and E-447.
{ECO:0000269|PubMed:9445476}.
MUTAGEN 441 441 S->E: Facilitates phosphorylation of T-
252 by PDPK1; when associated with E-412;
E-434; E-444 and E-447.
{ECO:0000269|PubMed:9445476}.
MUTAGEN 444 444 T->E: Facilitates phosphorylation of T-
252 by PDPK1; when associated with E-412;
E-434; E-441 and E-447.
{ECO:0000269|PubMed:9445476}.
MUTAGEN 447 447 S->E: Facilitates phosphorylation of T-
252 by PDPK1; when associated with E-412;
E-434; E-441 and E-444.
{ECO:0000269|PubMed:9445476}.
CONFLICT 222 222 E -> V (in Ref. 2; BAG61973).
{ECO:0000305}.
CONFLICT 428 428 F -> L (in Ref. 2; BAG35726).
{ECO:0000305}.
HELIX 88 90 {ECO:0000244|PDB:3WF7}.
STRAND 91 99 {ECO:0000244|PDB:3WF7}.
STRAND 101 110 {ECO:0000244|PDB:3WF7}.
TURN 114 117 {ECO:0000244|PDB:3WF7}.
STRAND 119 126 {ECO:0000244|PDB:3WF7}.
HELIX 127 132 {ECO:0000244|PDB:3WF7}.
HELIX 137 149 {ECO:0000244|PDB:3WF7}.
STRAND 158 164 {ECO:0000244|PDB:3WF7}.
STRAND 167 173 {ECO:0000244|PDB:3WF7}.
HELIX 180 187 {ECO:0000244|PDB:3WF7}.
HELIX 192 212 {ECO:0000244|PDB:3WF7}.
HELIX 221 223 {ECO:0000244|PDB:3WF7}.
STRAND 224 226 {ECO:0000244|PDB:3WF7}.
STRAND 232 234 {ECO:0000244|PDB:3WF7}.
STRAND 246 249 {ECO:0000244|PDB:3WF8}.
STRAND 252 255 {ECO:0000244|PDB:3WF7}.
HELIX 262 265 {ECO:0000244|PDB:3WF7}.
TURN 266 269 {ECO:0000244|PDB:4RLO}.
HELIX 273 288 {ECO:0000244|PDB:3WF7}.
HELIX 298 307 {ECO:0000244|PDB:3WF7}.
STRAND 314 316 {ECO:0000244|PDB:3A61}.
HELIX 318 327 {ECO:0000244|PDB:3WF7}.
HELIX 332 334 {ECO:0000244|PDB:3WF7}.
TURN 340 342 {ECO:0000244|PDB:3WF7}.
HELIX 343 347 {ECO:0000244|PDB:3WF7}.
HELIX 350 352 {ECO:0000244|PDB:3WF7}.
HELIX 357 361 {ECO:0000244|PDB:3WF7}.
TURN 371 373 {ECO:0000244|PDB:3WF7}.
STRAND 374 377 {ECO:0000244|PDB:4L44}.
TURN 380 382 {ECO:0000244|PDB:4L45}.
HELIX 409 411 {ECO:0000244|PDB:4L42}.
STRAND 413 415 {ECO:0000244|PDB:4L42}.
HELIX 418 421 {ECO:0000244|PDB:5WBH}.
HELIX 423 426 {ECO:0000244|PDB:5WBH}.
HELIX 429 431 {ECO:0000244|PDB:5WBH}.
SEQUENCE 525 AA; 59140 MW; 2C3BA13CCDAF4AB3 CRC64;
MRRRRRRDGF YPAPDFRDRE AEDMAGVFDI DLDQPEDAGS EDELEEGGQL NESMDHGGVG
PYELGMEHCE KFEISETSVN RGPEKIRPEC FELLRVLGKG GYGKVFQVRK VTGANTGKIF
AMKVLKKAMI VRNAKDTAHT KAERNILEEV KHPFIVDLIY AFQTGGKLYL ILEYLSGGEL
FMQLEREGIF MEDTACFYLA EISMALGHLH QKGIIYRDLK PENIMLNHQG HVKLTDFGLC
KESIHDGTVT HTFCGTIEYM APEILMRSGH NRAVDWWSLG ALMYDMLTGA PPFTGENRKK
TIDKILKCKL NLPPYLTQEA RDLLKKLLKR NAASRLGAGP GDAGEVQAHP FFRHINWEEL
LARKVEPPFK PLLQSEEDVS QFDSKFTRQT PVDSPDDSTL SESANQVFLG FTYVAPSVLE
SVKEKFSFEP KIRSPRRFIG SPRTPVSPVK FSPGDFWGRG ASASTANPQT PVEYPMETSG
IEQMDVTMSG EASAPLPIRQ PNSGPYKKQA FPMISKRPEH LRMNL


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Gentaur; yes we can

Pathways :
WP210: Cytoplasmic Ribosomal Proteins
WP32: Translation Factors
WP1493: Carbon assimilation C4 pathway
WP1566: Citrate cycle (TCA cycle)
WP2199: Seed Development
WP1531: Vitamin D synthesis
WP1567: Glycolysis and Gluconeogenesis
WP1619: Amino sugar and nucleotide sugar metabolism
WP1653: Galactose metabolism
WP1659: Glycine, serine and threonine metabolism
WP1681: Pantothenate and CoA biosynthesis
WP1701: Starch and sucrose metabolism
WP1703: Streptomycin biosynthesis
WP1844: MAP kinase cascade
WP1946: Cori Cycle
WP2218: sGC
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP253: Glycolysis
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling
WP1434: Osteopontin Signaling
WP1571: EBV LMP1 signaling
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation

Related Genes :
[RPS6KA1 MAPKAPK1A RSK1] Ribosomal protein S6 kinase alpha-1 (S6K-alpha-1) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (p90RSK1) (p90S6K) (MAP kinase-activated protein kinase 1a) (MAPK-activated protein kinase 1a) (MAPKAP kinase 1a) (MAPKAPK-1a) (Ribosomal S6 kinase 1) (RSK-1)
[Rps6ka1 Mapkapk1a Rsk1] Ribosomal protein S6 kinase alpha-1 (S6K-alpha-1) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (p90RSK1) (p90S6K) (MAP kinase-activated protein kinase 1a) (MAPK-activated protein kinase 1a) (MAPKAP kinase 1a) (MAPKAPK-1a) (Ribosomal S6 kinase 1) (RSK-1)
[Rps6ka1 Mapkapk1a Rsk1] Ribosomal protein S6 kinase alpha-1 (S6K-alpha-1) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (p90RSK1) (p90S6K) (MAP kinase-activated protein kinase 1a) (MAPK-activated protein kinase 1a) (MAPKAP kinase 1a) (MAPKAPK-1a) (Ribosomal S6 kinase 1) (RSK-1)
[Rps6ka3 Mapkapk1b Rps6ka-rs1 Rsk2] Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)
[RPS6KA3 ISPK1 MAPKAPK1B RSK2] Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (Insulin-stimulated protein kinase 1) (ISPK-1) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)
[RPS6KA2 MAPKAPK1C RSK3] Ribosomal protein S6 kinase alpha-2 (S6K-alpha-2) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 2) (p90-RSK 2) (p90RSK2) (MAP kinase-activated protein kinase 1c) (MAPK-activated protein kinase 1c) (MAPKAP kinase 1c) (MAPKAPK-1c) (Ribosomal S6 kinase 3) (RSK-3) (pp90RSK3)
[Rps6ka2 Mapkapk1c Rsk3] Ribosomal protein S6 kinase alpha-2 (S6K-alpha-2) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 2) (p90-RSK 2) (p90RSK2) (MAP kinase-activated protein kinase 1c) (MAPK-activated protein kinase 1c) (MAPKAP kinase 1c) (MAPKAPK-1c) (Protein-tyrosine kinase Mpk-9) (Ribosomal S6 kinase 3) (RSK-3) (pp90RSK3)
[ATPK1 ATPK6 S6K1 At3g08730 F17O14.20] Serine/threonine-protein kinase AtPK1/AtPK6 (EC 2.7.11.1) (Ribosomal-protein S6 kinase homolog 1)
[RPS6KA6 RSK4] Ribosomal protein S6 kinase alpha-6 (S6K-alpha-6) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 6) (p90-RSK 6) (p90RSK6) (Ribosomal S6 kinase 4) (RSK-4) (pp90RSK4)
[RPS6KA5 MSK1] Ribosomal protein S6 kinase alpha-5 (S6K-alpha-5) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 5) (Nuclear mitogen- and stress-activated protein kinase 1) (RSK-like protein kinase) (RSKL)
[Rps6ka5 Msk1] Ribosomal protein S6 kinase alpha-5 (S6K-alpha-5) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 5) (Nuclear mitogen- and stress-activated protein kinase 1) (RSK-like protein kinase) (RLSK)
[RPS6KA4 MSK2] Ribosomal protein S6 kinase alpha-4 (S6K-alpha-4) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 4) (Nuclear mitogen- and stress-activated protein kinase 2) (Ribosomal protein kinase B) (RSKB)
[Rps6ka4 Msk2] Ribosomal protein S6 kinase alpha-4 (S6K-alpha-4) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 4) (Nuclear mitogen- and stress-activated protein kinase 2) (RSK-like protein kinase) (RLSK)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

Bibliography :
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