KS6B1_MOUSE
ID KS6B1_MOUSE Reviewed; 525 AA.
AC Q8BSK8; Q5SWG1; Q8CHX0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Ribosomal protein S6 kinase beta-1;
DE Short=S6K-beta-1;
DE Short=S6K1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:11500364};
DE AltName: Full=70 kDa ribosomal protein S6 kinase 1;
DE Short=P70S6K1;
DE Short=p70-S6K 1;
DE AltName: Full=Ribosomal protein S6 kinase I;
DE Short=S6K;
DE AltName: Full=p70 ribosomal S6 kinase alpha;
DE Short=p70 S6 kinase alpha;
DE Short=p70 S6K-alpha;
DE Short=p70 S6KA;
GN Name=Rps6kb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION IN PHOSPHORYLATION OF EEF2K, AND CATALYTIC ACTIVITY.
RX PubMed=11500364; DOI=10.1093/emboj/20.16.4370;
RA Wang X., Li W., Williams M., Terada N., Alessi D.R., Proud C.G.;
RT "Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase.";
RL EMBO J. 20:4370-4379(2001).
RN [6]
RP FUNCTION IN PHOSPHORYLATION OF BAD, FUNCTION IN APOPTOSIS REGULATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11493700; DOI=10.1073/pnas.171301998;
RA Harada H., Andersen J.S., Mann M., Terada N., Korsmeyer S.J.;
RT "p70S6 kinase signals cell survival as well as growth, inactivating the
RT pro-apoptotic molecule BAD.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9666-9670(2001).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15060135; DOI=10.1128/mcb.24.8.3112-3124.2004;
RA Pende M., Um S.H., Mieulet V., Sticker M., Goss V.L., Mestan J.,
RA Mueller M., Fumagalli S., Kozma S.C., Thomas G.;
RT "S6K1(-/-)/S6K2(-/-) mice exhibit perinatal lethality and rapamycin-
RT sensitive 5'-terminal oligopyrimidine mRNA translation and reveal a
RT mitogen-activated protein kinase-dependent S6 kinase pathway.";
RL Mol. Cell. Biol. 24:3112-3124(2004).
RN [8]
RP FUNCTION IN PHOSPHORYLATION OF IRS1.
RX PubMed=18952604; DOI=10.1074/jbc.m806480200;
RA Zhang J., Gao Z., Yin J., Quon M.J., Ye J.;
RT "S6K directly phosphorylates IRS-1 on Ser-270 to promote insulin resistance
RT in response to TNF-(alpha) signaling through IKK2.";
RL J. Biol. Chem. 283:35375-35382(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447 AND SER-452, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION IN PHOSPHORYLATION OF EPRS.
RX PubMed=28178239; DOI=10.1038/nature21380;
RA Arif A., Terenzi F., Potdar A.A., Jia J., Sacks J., China A., Halawani D.,
RA Vasu K., Li X., Brown J.M., Chen J., Kozma S.C., Thomas G., Fox P.L.;
RT "EPRS is a critical mTORC1-S6K1 effector that influences adiposity in
RT mice.";
RL Nature 542:357-361(2017).
CC -!- FUNCTION: Serine/threonine-protein kinase that acts downstream of mTOR
CC signaling in response to growth factors and nutrients to promote cell
CC proliferation, cell growth and cell cycle progression. Regulates
CC protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and
CC contributes to cell survival by repressing the pro-apoptotic function
CC of BAD. Under conditions of nutrient depletion, the inactive form
CC associates with the EIF3 translation initiation complex. Upon mitogenic
CC stimulation, phosphorylation by the mammalian target of rapamycin
CC complex 1 (mTORC1) leads to dissociation from the EIF3 complex and
CC activation. The active form then phosphorylates and activates several
CC substrates in the pre-initiation complex, including the EIF2B complex
CC and the cap-binding complex component EIF4B. Also controls translation
CC initiation by phosphorylating a negative regulator of EIF4A, PDCD4,
CC targeting it for ubiquitination and subsequent proteolysis. Promotes
CC initiation of the pioneer round of protein synthesis by phosphorylating
CC POLDIP3/SKAR. In response to IGF1, activates translation elongation by
CC phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and
CC thus activation of EEF2. Also plays a role in feedback regulation of
CC mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition
CC of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating
CC the pro-apoptotic protein BAD and suppressing its pro-apoptotic
CC function. Phosphorylates mitochondrial RMP leading to dissociation of a
CC RMP:PPP1CC complex. The free mitochondrial PPP1CC can then
CC dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative
CC feedback mechanism for the RPS6KB1 anti-apoptotic function. Mediates
CC TNF-alpha-induced insulin resistance by phosphorylating IRS1 at
CC multiple serine residues, resulting in accelerated degradation of IRS1.
CC In cells lacking functional TSC1-2 complex, constitutively
CC phosphorylates and inhibits GSK3B. May be involved in cytoskeletal
CC rearrangement through binding to neurabin. Phosphorylates and activates
CC the pyrimidine biosynthesis enzyme CAD, downstream of MTOR (By
CC similarity) (PubMed:11493700, PubMed:11500364, PubMed:15060135,
CC PubMed:18952604). Following activation by mTORC1, phosphorylates EPRS
CC and thereby plays a key role in fatty acid uptake by adipocytes and
CC also most probably in interferon-gamma-induced translation inhibition
CC (PubMed:28178239). {ECO:0000250|UniProtKB:P23443,
CC ECO:0000269|PubMed:11493700, ECO:0000269|PubMed:11500364,
CC ECO:0000269|PubMed:15060135, ECO:0000269|PubMed:18952604,
CC ECO:0000269|PubMed:28178239}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:11500364};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11500364};
CC -!- ACTIVITY REGULATION: Activation requires multiple phosphorylation
CC events on serine/threonine residues. Activation appears to be first
CC mediated by phosphorylation of multiple sites in the autoinhibitory
CC domain, which facilitates phosphorylation at Thr-412, disrupting the
CC autoinhibitory mechanism and allowing phosphorylation of Thr-252 by
CC PDPK1. The active conformation of the kinase is believed to be
CC stabilized by a mechanism involving three conserved phosphorylation
CC sites located in the kinase domain activation loop (Thr-252) and in the
CC AGC-kinase C-terminal domain (Ser-394 in the middle of the tail/linker
CC region and Thr-412 within a hydrophobic motif at its end). Activated by
CC mTORC1; isoform Alpha I and isoform Alpha II are sensitive to
CC rapamycin, which inhibits activating phosphorylation at Thr-412.
CC Activated by PDPK1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1R9A/neurabin-1. Interacts with RPTOR.
CC Interacts with IRS1. Interacts with EIF3B and EIF3C. Interacts with
CC TRAF4. Interacts with POLDIP3. Interacts (via N-terminus) with IER5.
CC {ECO:0000250|UniProtKB:P23443, ECO:0000250|UniProtKB:P67999}.
CC -!- INTERACTION:
CC Q8BSK8; P23804: Mdm2; NbExp=2; IntAct=EBI-646423, EBI-641788;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse, synaptosome
CC {ECO:0000250}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:11493700}. Mitochondrion {ECO:0000250}.
CC Note=Colocalizes with URI1 at mitochondrion. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Alpha I;
CC IsoId=Q8BSK8-1; Sequence=Displayed;
CC Name=Alpha II;
CC IsoId=Q8BSK8-2; Sequence=VSP_018840;
CC -!- DOMAIN: The autoinhibitory domain is believed to block phosphorylation
CC within the AGC-kinase C-terminal domain and the activation loop.
CC {ECO:0000250}.
CC -!- DOMAIN: The TOS (TOR signaling) motif is essential for activation by
CC mTORC1. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Thr-412 is regulated by mTORC1. The
CC phosphorylation at this site is maintained by an agonist-dependent
CC autophosphorylation mechanism. Activated by phosphorylation at Thr-252
CC by PDPK1. Dephosphorylation by PPP1CC at Thr-412 in mitochondrion (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Impairment of body growth. Lethal in combination
CC with Rps6kb2 deficiency. {ECO:0000269|PubMed:15060135}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. S6 kinase subfamily. {ECO:0000305}.
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DR EMBL; AK032724; BAC28000.1; -; mRNA.
DR EMBL; AL604063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL15788.1; -; Genomic_DNA.
DR EMBL; BC038491; AAH38491.1; -; mRNA.
DR CCDS; CCDS48875.1; -. [Q8BSK8-1]
DR RefSeq; NP_001107806.1; NM_001114334.1. [Q8BSK8-1]
DR AlphaFoldDB; Q8BSK8; -.
DR SMR; Q8BSK8; -.
DR BioGRID; 215408; 11.
DR IntAct; Q8BSK8; 6.
DR MINT; Q8BSK8; -.
DR STRING; 10090.ENSMUSP00000119715; -.
DR ChEMBL; CHEMBL5429; -.
DR iPTMnet; Q8BSK8; -.
DR PhosphoSitePlus; Q8BSK8; -.
DR EPD; Q8BSK8; -.
DR MaxQB; Q8BSK8; -.
DR PaxDb; Q8BSK8; -.
DR PRIDE; Q8BSK8; -.
DR ProteomicsDB; 264878; -. [Q8BSK8-1]
DR ProteomicsDB; 264879; -. [Q8BSK8-2]
DR Antibodypedia; 3544; 2693 antibodies from 54 providers.
DR DNASU; 72508; -.
DR Ensembl; ENSMUST00000154617; ENSMUSP00000119715; ENSMUSG00000020516. [Q8BSK8-1]
DR GeneID; 72508; -.
DR KEGG; mmu:72508; -.
DR UCSC; uc007ksn.2; mouse. [Q8BSK8-1]
DR CTD; 6198; -.
DR MGI; MGI:1270849; Rps6kb1.
DR VEuPathDB; HostDB:ENSMUSG00000020516; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000154203; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; Q8BSK8; -.
DR OMA; KGSIFAM; -.
DR PhylomeDB; Q8BSK8; -.
DR TreeFam; TF313438; -.
DR Reactome; R-MMU-166208; mTORC1-mediated signalling.
DR BioGRID-ORCS; 72508; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Rps6kb1; mouse.
DR PRO; PR:Q8BSK8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BSK8; protein.
DR Bgee; ENSMUSG00000020516; Expressed in lacrimal gland and 266 other tissues.
DR ExpressionAtlas; Q8BSK8; baseline and differential.
DR Genevisible; Q8BSK8; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:MGI.
DR GO; GO:0004711; F:ribosomal protein S6 kinase activity; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0001662; P:behavioral fear response; IGI:MGI.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IMP:UniProtKB.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0007281; P:germ cell development; IDA:MGI.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; IMP:UniProtKB.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISO:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IGI:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0046324; P:regulation of glucose import; ISO:MGI.
DR GO; GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; ISO:MGI.
DR GO; GO:0043201; P:response to leucine; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0031667; P:response to nutrient levels; ISO:MGI.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0014732; P:skeletal muscle atrophy; IEA:Ensembl.
DR GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
DR GO; GO:0031929; P:TOR signaling; ISS:UniProtKB.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016238; Ribosomal_S6_kinase.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000605; Ribsml_S6_kin_1; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Apoptosis; ATP-binding; Cell cycle;
KW Cytoplasm; Kinase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Synapse; Synaptosome; Transferase;
KW Translation regulation.
FT CHAIN 1..525
FT /note="Ribosomal protein S6 kinase beta-1"
FT /id="PRO_0000024344"
FT DOMAIN 91..352
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 353..423
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 32..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..525
FT /note="Autoinhibitory domain"
FT MOTIF 28..32
FT /note="TOS motif"
FT COMPBIAS 32..48
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 97..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 252
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:P23443"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23443"
FT MOD_RES 412
FT /note="Phosphothreonine; by MTOR, NEK6 and NEK7"
FT /evidence="ECO:0000250|UniProtKB:P67999"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P67999"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23443"
FT MOD_RES 444
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P23443"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 516
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P67999"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform Alpha II)"
FT /evidence="ECO:0000305"
FT /id="VSP_018840"
FT CONFLICT 60
FT /note="G -> E (in Ref. 1; BAC28000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 59146 MW; 5B3C09F6BB365EE2 CRC64;
MRRRRRRDGF YLAPDFRHRE 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
IEQMDVTVSG EASAPLPIRQ PNSGPYKKQA FPMISKRPEH LRMNL
