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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) (p70 ribosomal S6 kinase alpha) (p70 S6 kinase alpha) (p70 S6K-alpha) (p70 S6KA)

 KS6B1_RAT               Reviewed;         525 AA.
P67999; P21425;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
27-SEP-2017, entry version 131.
RecName: Full=Ribosomal protein S6 kinase beta-1;
Short=S6K-beta-1;
Short=S6K1;
EC=2.7.11.1;
AltName: Full=70 kDa ribosomal protein S6 kinase 1;
Short=P70S6K1;
Short=p70-S6K 1;
AltName: Full=Ribosomal protein S6 kinase I;
AltName: Full=p70 ribosomal S6 kinase alpha;
Short=p70 S6 kinase alpha;
Short=p70 S6K-alpha;
Short=p70 S6KA;
Name=Rps6kb1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2236064; DOI=10.1073/pnas.87.21.8550;
Banerjee P., Ahmad M.F., Grove J.R., Kozlosky C., Price D.J.,
Avruch J.;
"Molecular structure of a major insulin/mitogen-activated 70-kDa S6
protein kinase.";
Proc. Natl. Acad. Sci. U.S.A. 87:8550-8554(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 24-525, AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Sprague-Dawley;
PubMed=1699226; DOI=10.1073/pnas.87.19.7365;
Kozma S.C., Ferrari S., Bassand P., Siegmann M., Totty N., Thomas G.;
"Cloning of the mitogen-activated S6 kinase from rat liver reveals an
enzyme of the second messenger subfamily.";
Proc. Natl. Acad. Sci. U.S.A. 87:7365-7369(1990).
[3]
FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF LYS-123; SER-434;
SER-441; THR-444 AND SER-447.
PubMed=8524831; DOI=10.1073/pnas.92.25.11696;
Cheatham L., Monfar M., Chou M.M., Blenis J.;
"Structural and functional analysis of pp70S6k.";
Proc. Natl. Acad. Sci. U.S.A. 92:11696-11700(1995).
[4]
ENZYME REGULATION.
PubMed=9427642; DOI=10.1016/S0960-9822(98)70037-5;
Alessi D.R., Kozlowski M.T., Weng Q.P., Morrice N., Avruch J.;
"3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates
and activates the p70 S6 kinase in vivo and in vitro.";
Curr. Biol. 8:69-81(1998).
[5]
PHOSPHORYLATION AT THR-252; SER-394; THR-412; SER-434; THR-444 AND
SER-447, AND MUTAGENESIS OF LYS-123; THR-252; THR-256; SER-394 AND
THR-412.
PubMed=9632736; DOI=10.1074/jbc.273.26.16621;
Weng Q.P., Kozlowski M., Belham C., Zhang A., Comb M.J., Avruch J.;
"Regulation of the p70 S6 kinase by phosphorylation in vivo. Analysis
using site-specific anti-phosphopeptide antibodies.";
J. Biol. Chem. 273:16621-16629(1998).
[6]
PHOSPHORYLATION AT THR-412 BY MTOR.
PubMed=9465032; DOI=10.1073/pnas.95.4.1432;
Burnett P.E., Barrow R.K., Cohen N.A., Snyder S.H., Sabatini D.M.;
"RAFT1 phosphorylation of the translational regulators p70 S6 kinase
and 4E-BP1.";
Proc. Natl. Acad. Sci. U.S.A. 95:1432-1437(1998).
[7]
INTERACTION WITH NEURABIN-I, AND MUTAGENESIS.
PubMed=9653190; DOI=10.1073/pnas.95.14.8351;
Burnett P.E., Blackshaw S., Lai M.M., Qureshi I.A., Burnett A.F.,
Sabatini D.M., Snyder S.H.;
"Neurabin is a synaptic protein linking p70 S6 kinase and the neuronal
cytoskeleton.";
Proc. Natl. Acad. Sci. U.S.A. 95:8351-8356(1998).
[8]
PHOSPHORYLATION AT THR-412.
PubMed=11516946; DOI=10.1016/S0960-9822(01)00369-4;
Belham C., Comb M.J., Avruch J.;
"Identification of the NIMA family kinases NEK6/7 as regulators of the
p70 ribosomal S6 kinase.";
Curr. Biol. 11:1155-1167(2001).
[9]
INTERACTION WITH RPTOR, TOS MOTIF, AND MUTAGENESIS OF PHE-28; ASP-29;
ILE-30; ASP-31 AND LEU-32.
PubMed=11967149; DOI=10.1016/S0960-9822(02)00762-5;
Schalm S.S., Blenis J.;
"Identification of a conserved motif required for mTOR signaling.";
Curr. Biol. 12:632-639(2002).
[10]
AUTOPHOSPHORYLATION.
PubMed=12183455; DOI=10.1074/jbc.M205168200;
Romanelli A., Dreisbach V.C., Blenis J.;
"Characterization of phosphatidylinositol 3-kinase-dependent
phosphorylation of the hydrophobic motif site Thr(389) in p70 S6
kinase 1.";
J. Biol. Chem. 277:40281-40289(2002).
[11]
INTERACTION WITH RPTOR, AND MUTAGENESIS OF PHE-28.
PubMed=12604610; DOI=10.1074/jbc.C200665200;
Nojima H., Tokunaga C., Eguchi S., Oshiro N., Hidayat S., Yoshino K.,
Hara K., Tanaka N., Avruch J., Yonezawa K.;
"The mammalian target of rapamycin (mTOR) partner, raptor, binds the
mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling
(TOS) motif.";
J. Biol. Chem. 278:15461-15464(2003).
[12]
ACETYLATION AT LYS-516.
PubMed=20599721; DOI=10.1016/j.bbrc.2010.06.081;
Fenton T.R., Gwalter J., Cramer R., Gout I.T.;
"S6K1 is acetylated at lysine 516 in response to growth factor
stimulation.";
Biochem. Biophys. Res. Commun. 398:400-405(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447 AND SER-452, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 preinitiation 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 RMP leading
to dissociation of a RMP: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 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:8524831}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with PPP1R9A/neurabin-1 (PubMed:9653190).
Interacts with RPTOR (PubMed:11967149, PubMed:12604610). Interacts
with IRS1 (By similarity). Interacts with EIF3B and EIF3C (By
similarity). Interacts with POLDIP3 (By similarity). Interacts
with TRAF4 (By similarity). Interacts (via N-terminus) with IER5
(By similarity). {ECO:0000250|UniProtKB:P23443,
ECO:0000269|PubMed:11967149, ECO:0000269|PubMed:12604610,
ECO:0000269|PubMed:9653190}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-2639458, EBI-2639458;
O35867:Ppp1r9a; NbExp=4; IntAct=EBI-2639458, EBI-7092421;
Q8N122:RPTOR (xeno); NbExp=2; IntAct=EBI-2639458, EBI-1567928;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse,
synaptosome. Mitochondrion outer membrane. Mitochondrion
{ECO:0000250}. Note=Colocalizes with URI1 at mitochondrion.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Alpha I;
IsoId=P67999-1; Sequence=Displayed;
Name=Alpha II;
IsoId=P67999-2; Sequence=VSP_018842;
-!- TISSUE SPECIFICITY: Brain.
-!- 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.
-!- PTM: Dephosphorylation by PPP1CC at Thr-412 in mitochondrion (By
similarity). Phosphorylation at Thr-412 is regulated by mTORC1.
The phosphorylation at this site is maintained by an agonist-
dependent autophosphorylation mechanism. Activated by
phosphorylation at Thr-252 by PDPK1. {ECO:0000250,
ECO:0000269|PubMed:11516946, ECO:0000269|PubMed:9465032,
ECO:0000269|PubMed:9632736}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. S6 kinase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M58340; AAA42104.1; -; mRNA.
EMBL; M57428; AAA42103.1; -; mRNA.
PIR; A36484; TVRTK6.
RefSeq; NP_114191.1; NM_031985.1.
UniGene; Rn.4042; -.
ProteinModelPortal; P67999; -.
SMR; P67999; -.
BioGrid; 249866; 3.
ELM; P67999; -.
IntAct; P67999; 7.
MINT; MINT-1212774; -.
STRING; 10116.ENSRNOP00000005226; -.
iPTMnet; P67999; -.
PhosphoSitePlus; P67999; -.
PaxDb; P67999; -.
PRIDE; P67999; -.
Ensembl; ENSRNOT00000005226; ENSRNOP00000005226; ENSRNOG00000003919. [P67999-1]
GeneID; 83840; -.
KEGG; rno:83840; -.
CTD; 6198; -.
RGD; 620683; Rps6kb1.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00890000139324; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; P67999; -.
KO; K04688; -.
OMA; HGGVGQY; -.
OrthoDB; EOG091G05Z7; -.
PhylomeDB; P67999; -.
TreeFam; TF313438; -.
BRENDA; 2.7.11.1; 5301.
Reactome; R-RNO-166208; mTORC1-mediated signalling.
SABIO-RK; P67999; -.
PRO; PR:P67999; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000003919; -.
Genevisible; P67999; RN.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:0004672; F:protein kinase activity; IDA:RGD.
GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:Ensembl.
GO; GO:0004711; F:ribosomal protein S6 kinase activity; IMP:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0016477; P:cell migration; IEP:RGD.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0007281; P:germ cell development; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007616; P:long-term memory; IEP:RGD.
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:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; IMP:RGD.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0045948; P:positive regulation of translational initiation; IBA:GO_Central.
GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0046324; P:regulation of glucose import; IMP:UniProtKB.
GO; GO:0043200; P:response to amino acid; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0033762; P:response to glucagon; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0009408; P:response to heat; IEP:RGD.
GO; GO:0032868; P:response to insulin; IMP:UniProtKB.
GO; GO:0043201; P:response to leucine; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0033574; P:response to testosterone; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0034612; P:response to tumor necrosis factor; IMP:UniProtKB.
GO; GO:0009611; P:response to wounding; IEP:RGD.
GO; GO:0014732; P:skeletal muscle atrophy; IEP:RGD.
GO; GO:0003009; P:skeletal muscle contraction; IEP:RGD.
GO; GO:0031929; P:TOR signaling; IEA:Ensembl.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom.
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.
PANTHER; PTHR24351:SF121; PTHR24351:SF121; 1.
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;
Acetylation; Alternative initiation; Apoptosis; ATP-binding;
Cell cycle; Cell junction; Complete proteome; Cytoplasm;
Direct protein sequencing; Kinase; Membrane; Mitochondrion;
Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Synapse;
Synaptosome; Transferase; Translation regulation.
CHAIN 1 525 Ribosomal protein S6 kinase beta-1.
/FTId=PRO_0000024348.
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:9632736}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000269|PubMed:9632736}.
MOD_RES 412 412 Phosphothreonine; by MTOR, NEK6 and NEK7.
{ECO:0000269|PubMed:11516946,
ECO:0000269|PubMed:9465032,
ECO:0000269|PubMed:9632736}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000269|PubMed:9632736}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:P23443}.
MOD_RES 444 444 Phosphothreonine.
{ECO:0000269|PubMed:9632736}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:9632736}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 516 516 N6-acetyllysine.
{ECO:0000269|PubMed:20599721}.
VAR_SEQ 1 23 Missing (in isoform Alpha II).
{ECO:0000305}.
/FTId=VSP_018842.
MUTAGEN 28 32 Missing: Almost complete loss of
activity.
MUTAGEN 28 28 F->A: Complete loss of activity.
Abolishes interaction with RPTOR. Reduces
phosphorylation. Loss of phosphorylation
at T-412 and T-444.
{ECO:0000269|PubMed:11967149,
ECO:0000269|PubMed:12604610}.
MUTAGEN 29 29 D->A: Almost complete loss of activity;
when associated with A-31.
{ECO:0000269|PubMed:11967149}.
MUTAGEN 30 30 I->A: Almost complete loss of activity;
when associated with A-32.
{ECO:0000269|PubMed:11967149}.
MUTAGEN 31 31 D->A: Almost complete loss of activity;
when associated with A-29.
{ECO:0000269|PubMed:11967149}.
MUTAGEN 32 32 L->A: Almost complete loss of activity;
when associated with A-30.
{ECO:0000269|PubMed:11967149}.
MUTAGEN 123 123 K->M: Loss of activity towards ribosomal
protein S6. {ECO:0000269|PubMed:8524831,
ECO:0000269|PubMed:9632736}.
MUTAGEN 123 123 K->R: Loss of activity.
{ECO:0000269|PubMed:8524831,
ECO:0000269|PubMed:9632736}.
MUTAGEN 252 252 T->A: Loss of activity towards ribosomal
protein S6 and reduced phosphorylation at
Thr-412. {ECO:0000269|PubMed:9632736}.
MUTAGEN 256 256 T->A: Loss of activity towards ribosomal
protein S6 without effect on
phosphorylation status.
{ECO:0000269|PubMed:9632736}.
MUTAGEN 394 394 S->A,D: Loss of activity towards
ribosomal protein S6 and reduces
phosphorylation at Thr-252.
{ECO:0000269|PubMed:9632736}.
MUTAGEN 412 412 T->A: Loss of activity towards ribosomal
protein S6 and loss of phosphorylation at
Thr-252. {ECO:0000269|PubMed:9632736}.
MUTAGEN 412 412 T->E: Mimics phosphorylation.
Constitutive active. No effect on
activity towards ribosomal protein S6.
{ECO:0000269|PubMed:9632736}.
MUTAGEN 434 434 S->D: No effect on sensitivity to
wortmannin and rapamycin; when associated
with D-441, D-444 and D-447.
{ECO:0000269|PubMed:8524831}.
MUTAGEN 441 441 S->D: No effect on sensitivity to
wortmannin and rapamycin; when associated
with D-434, D-D-444 and D-447.
{ECO:0000269|PubMed:8524831}.
MUTAGEN 444 444 T->D: No effect on sensitivity to
wortmannin and rapamycin; when associated
with D-434, D-441, and D-447.
{ECO:0000269|PubMed:8524831}.
MUTAGEN 447 447 S->D: No effect on sensitivity to
wortmannin and rapamycin; when associated
with D-434, D-441 and D-444.
{ECO:0000269|PubMed:8524831}.
CONFLICT 367 367 P -> R (in Ref. 1; AAA42104).
{ECO:0000305}.
SEQUENCE 525 AA; 59132 MW; 013BA13EFB3508D7 CRC64;
MRRRRRRDGF YPAPDFRHRE 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
IEQMDVTTSG EASAPLPIRQ PNSGPYKKQA FPMISKRPEH LRMNL


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10-782-55114 Ribosomal protein S6 kinase beta-1 - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha N_A 0.001 mg
10-782-55114 Ribosomal protein S6 kinase beta-1 - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha N_A 0.005 mg
10-782-55114 Ribosomal protein S6 kinase beta-1 - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha N_A 0.01 mg
10-782-55114 Ribosomal protein S6 kinase beta-1 - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha N_A 0.02 mg
18-785-210339 p70 S6 Kinase (Phospho-Ser424) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.05 mg
18-785-210338 p70 S6 Kinase (Phospho-Ser411) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.1 mg
18-785-210338 p70 S6 Kinase (Phospho-Ser411) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.05 mg
18-785-210337 p70 S6 Kinase (Phospho-Thr421) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.1 mg
18-785-210339 p70 S6 Kinase (Phospho-Ser424) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.1 mg
18-785-210337 p70 S6 Kinase (Phospho-Thr421) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.05 mg
18-783-75538 RABBIT ANTI RIBOSOMAL S6 KINASE 2 (C-TERMINAL) - RIBOSOMAL PROTEIN S6 KINASE ALPHA-2; EC 2.7.11.1; S6K-alpha 2; 90 kDa ribosomal protein S6 kinase 2; p90-RSK 2; Ribosomal S6 kinase 3; RSK-3; pp90RSK3; 0.1 ml
18-785-210340 p70 S6 Kinase (Ab-389) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.05 mg
18-785-210342 p70 S6 Kinase (Ab-411) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.05 mg
18-785-210342 p70 S6 Kinase (Ab-411) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.1 mg
18-785-210341 p70 S6 Kinase (Ab-421) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.1 mg
18-785-210340 p70 S6 Kinase (Ab-389) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.1 mg
18-785-210343 p70 S6 Kinase (Ab-424) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.1 mg
18-785-210343 p70 S6 Kinase (Ab-424) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.05 mg
18-785-210341 p70 S6 Kinase (Ab-421) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.05 mg
20-272-191794 RPS6KB1 - Mouse monoclonal [1457Q15] to RPS6KB1; EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70- 0.1 mg
10-782-55112 Ribosomal protein S6 kinase alpha-1 - EC 2.7.11.1; S6K-alpha 1; 90 kDa ribosomal protein S6 kinase 1; p90-RSK 1; Ribosomal S6 kinase 1; RSK-1; pp90RSK1; p90S6K; MAP kinase-activated protein kinase 1a; 0.01 mg
10-782-55112 Ribosomal protein S6 kinase alpha-1 - EC 2.7.11.1; S6K-alpha 1; 90 kDa ribosomal protein S6 kinase 1; p90-RSK 1; Ribosomal S6 kinase 1; RSK-1; pp90RSK1; p90S6K; MAP kinase-activated protein kinase 1a; 0.02 mg
10-782-55112 Ribosomal protein S6 kinase alpha-1 - EC 2.7.11.1; S6K-alpha 1; 90 kDa ribosomal protein S6 kinase 1; p90-RSK 1; Ribosomal S6 kinase 1; RSK-1; pp90RSK1; p90S6K; MAP kinase-activated protein kinase 1a; 0.005 mg
10-782-55112 Ribosomal protein S6 kinase alpha-1 - EC 2.7.11.1; S6K-alpha 1; 90 kDa ribosomal protein S6 kinase 1; p90-RSK 1; Ribosomal S6 kinase 1; RSK-1; pp90RSK1; p90S6K; MAP kinase-activated protein kinase 1a; 0.001 mg
18-785-210346 p90RSK (Phospho-Thr348) - EC 2.7.11.1; S6K-alpha 1; 90 kDa ribosomal protein S6 kinase 1; p90-RSK 1; Ribosomal S6 kinase 1; RSK-1; pp90RSK1; p90S6K; MAP kinase-activated protein kinase 1a; MAPKAPK1A P 0.1 mg


 

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