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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)

 KS6A3_MOUSE             Reviewed;         740 AA.
P18654; B1AXN4; Q03140; Q8K3J8;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
25-MAR-2003, sequence version 2.
12-AUG-2020, entry version 202.
RecName: Full=Ribosomal protein S6 kinase alpha-3;
Short=S6K-alpha-3;
EC=2.7.11.1 {ECO:0000269|PubMed:15109498};
AltName: Full=90 kDa ribosomal protein S6 kinase 3;
Short=p90-RSK 3;
Short=p90RSK3;
AltName: Full=MAP kinase-activated protein kinase 1b;
Short=MAPK-activated protein kinase 1b;
Short=MAPKAP kinase 1b;
Short=MAPKAPK-1b;
AltName: Full=Ribosomal S6 kinase 2 {ECO:0000303|PubMed:15109498};
Short=RSK-2 {ECO:0000303|PubMed:15109498};
AltName: Full=pp90RSK2;
Name=Rps6ka3;
Synonyms=Mapkapk1b, Rps6ka-rs1, Rsk2 {ECO:0000303|PubMed:15109498};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12016217; DOI=10.1074/jbc.m202663200;
Chrestensen C.A., Sturgill T.W.;
"Characterization of the p90 ribosomal S6 kinase 2 carboxyl-terminal domain
as a protein kinase.";
J. Biol. Chem. 277:27733-27741(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 108-740.
PubMed=2779569; DOI=10.1128/mcb.9.9.3850;
Alcorta D.A., Crews C.M., Sweet L.J., Bankston L., Jones S.W.,
Erikson R.L.;
"Sequence and expression of chicken and mouse rsk: homologs of Xenopus
laevis ribosomal S6 kinase.";
Mol. Cell. Biol. 9:3850-3859(1989).
[4]
ACTIVITY REGULATION, PHOSPHORYLATION AT SER-227 AND SER-386, AND
MUTAGENESIS OF SER-227 AND SER-386.
PubMed=10480933; DOI=10.1074/jbc.274.38.27168;
Jensen C.J., Buch M.-B., Krag T.O., Hemmings B.A., Gammeltoft S.,
Froedin M.;
"90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-
phosphoinositide-dependent protein kinase-1.";
J. Biol. Chem. 274:27168-27176(1999).
[5]
FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF SER-386.
PubMed=10856237; DOI=10.1093/emboj/19.12.2924;
Froedin M., Jensen C.J., Merienne K., Gammeltoft S.;
"A phosphoserine-regulated docking site in the protein kinase RSK2 that
recruits and activates PDK1.";
EMBO J. 19:2924-2934(2000).
[6]
FUNCTION IN PHOSPHORYLATION OF CDKN1B.
PubMed=14504289; DOI=10.1074/jbc.m306614200;
Fujita N., Sato S., Tsuruo T.;
"Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6
kinases promotes its binding to 14-3-3 and cytoplasmic localization.";
J. Biol. Chem. 278:49254-49260(2003).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
PubMed=15109498; DOI=10.1016/s0092-8674(04)00344-7;
Yang X., Matsuda K., Bialek P., Jacquot S., Masuoka H.C., Schinke T.,
Li L., Brancorsini S., Sassone-Corsi P., Townes T.M., Hanauer A.,
Karsenty G.;
"ATF4 is a substrate of RSK2 and an essential regulator of osteoblast
biology; implication for Coffin-Lowry Syndrome.";
Cell 117:387-398(2004).
[8]
FUNCTION IN HEMATOPOIETIC TRANSFORMATION, PHOSPHORYLATION AT TYR-529, AND
MUTAGENESIS OF TYR-529.
PubMed=17785202; DOI=10.1016/j.ccr.2007.08.003;
Kang S., Dong S., Gu T.L., Guo A., Cohen M.S., Lonial S., Khoury H.J.,
Fabbro D., Gilliland D.G., Bergsagel P.L., Taunton J., Polakiewicz R.D.,
Chen J.;
"FGFR3 activates RSK2 to mediate hematopoietic transformation through
tyrosine phosphorylation of RSK2 and activation of the MEK/ERK pathway.";
Cancer Cell 12:201-214(2007).
[9]
FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING, AND PHOSPHORYLATION AT SER-386.
PubMed=17906627; DOI=10.1038/ni1517;
Zaru R., Ronkina N., Gaestel M., Arthur J.S., Watts C.;
"The MAPK-activated kinase Rsk controls an acute Toll-like receptor
signaling response in dendritic cells and is activated through two distinct
pathways.";
Nat. Immunol. 8:1227-1235(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369; SER-415 AND
SER-715, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[11]
FUNCTION.
PubMed=22827337; DOI=10.1042/bj20120938;
Saha M., Carriere A., Cheerathodi M., Zhang X., Lavoie G., Rush J.,
Roux P.P., Ballif B.A.;
"RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively
regulating MAPK activation.";
Biochem. J. 447:159-166(2012).
[12]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 399-740.
PubMed=18084304; DOI=10.1038/nsmb1347;
Malakhova M., Tereshko V., Lee S.Y., Yao K., Cho Y.Y., Bode A., Dong Z.;
"Structural basis for activation of the autoinhibitory C-terminal kinase
domain of p90 RSK2.";
Nat. Struct. Mol. Biol. 15:112-113(2008).
[13]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 44-367.
PubMed=19956600; DOI=10.1371/journal.pone.0008044;
Malakhova M., Kurinov I., Liu K., Zheng D., D'Angelo I., Shim J.H.,
Steinman V., Bode A.M., Dong Z.;
"Structural diversity of the active N-terminal kinase domain of p90
ribosomal S6 kinase 2.";
PLoS ONE 4:E8044-E8044(2009).
-!- FUNCTION: Serine/threonine-protein kinase that acts downstream of ERK
(MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and
stress-induced activation of the transcription factors CREB1, ETV1/ER81
and NR4A1/NUR77, regulates translation through RPS6 and EIF4B
phosphorylation, and mediates cellular proliferation, survival, and
differentiation by modulating mTOR signaling and repressing pro-
apoptotic function of BAD and DAPK1 (PubMed:10856237, PubMed:15109498).
In fibroblast, is required for EGF-stimulated phosphorylation of CREB1
and histone H3 at 'Ser-10', which results in the subsequent
transcriptional activation of several immediate-early genes (By
similarity). In response to mitogenic stimulation (EGF and PMA),
phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription
factors and the cofactor CREBBP (By similarity). Upon insulin-derived
signal, acts indirectly on the transcription regulation of several
genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity
(By similarity). Phosphorylates RPS6 in response to serum or EGF via an
mTOR-independent mechanism and promotes translation initiation by
facilitating assembly of the preinitiation complex (By similarity). In
response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for
the EIF3 complex and stimulating cap-dependent translation (By
similarity). Is involved in the mTOR nutrient-sensing pathway by
directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits
TSC2 ability to suppress mTOR signaling, and mediates phosphorylation
of RPTOR, which regulates mTORC1 activity and may promote rapamycin-
sensitive signaling independently of the PI3K/AKT pathway (By
similarity). Mediates cell survival by phosphorylating the pro-
apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic
function (By similarity). Promotes the survival of hepatic stellate
cells by phosphorylating CEBPB in response to the hepatotoxin carbon
tetrachloride (CCl4) (By similarity). Is involved in cell cycle
regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes
CDKN1B association with 14-3-3 proteins and prevents its translocation
to the nucleus and inhibition of G1 progression (PubMed:14504289). In
LPS-stimulated dendritic cells, is involved in TLR4-induced
macropinocytosis, and in myeloma cells, acts as effector of FGFR3-
mediated transformation signaling, after direct phosphorylation at Tyr-
529 by FGFR3 (PubMed:17785202, PubMed:17906627). Negatively regulates
EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1
(PubMed:22827337). Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161'
that create YWHAB and YWHAE binding sites and which contribute to the
negative regulation of MAPK1/3 phosphorylation (PubMed:22827337).
Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway
controls cell migration (By similarity). Acts as a regulator of
osteoblast differentiation by mediating phosphorylation of ATF4,
thereby promoting ATF4 transactivation activity (PubMed:15109498).
{ECO:0000250|UniProtKB:P51812, ECO:0000269|PubMed:10856237,
ECO:0000269|PubMed:14504289, ECO:0000269|PubMed:15109498,
ECO:0000269|PubMed:17785202, ECO:0000269|PubMed:17906627,
ECO:0000269|PubMed:22827337}.
-!- 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:15109498};
-!- 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;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: Upon extracellular signal or mitogen stimulation,
phosphorylated at Thr-577 in the C-terminal kinase domain (CTKD) by
MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates
Ser-386, allowing binding of PDPK1, which in turn phosphorylates Ser-
227 in the N-terminal kinase domain (NTDK) leading to the full
activation of the protein and subsequent phosphorylation of the
substrates by the NTKD (By similarity). {ECO:0000250}.
-!- SUBUNIT: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in
quiescent cells. Transiently dissociates following mitogenic
stimulation (By similarity). Interacts with NFATC4, ETV1/ER81 and FGFR1
(By similarity). {ECO:0000250}.
-!- INTERACTION:
P18654; P30309: cdc25-1-b; Xeno; NbExp=3; IntAct=EBI-397744, EBI-15888737;
P18654; P28223-1: HTR2A; Xeno; NbExp=2; IntAct=EBI-397744, EBI-15573967;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51812}. Cytoplasm
{ECO:0000250|UniProtKB:P51812}.
-!- TISSUE SPECIFICITY: Intestine, thymus, lung, heart and brain.
-!- PTM: Activated by phosphorylation at Ser-227 by PDPK1.
Autophosphorylated on Ser-386, as part of the activation process. May
be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and MAPK3/ERK1.
Can also be activated via phosphorylation at Ser-386 by MAPKAPK2.
{ECO:0000269|PubMed:10480933, ECO:0000269|PubMed:17785202,
ECO:0000269|PubMed:17906627}.
-!- PTM: N-terminal myristoylation results in an activated kinase in the
absence of added growth factors. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice were born at expected Mendelian ratio but
display decreased bone mass (PubMed:15109498). Embryos and pups show a
delay in mineralization of the skull with frontal, parietal, and
interparietal bones of reduced size (PubMed:15109498). Mice also
display a significant reduction in long bone length at one month of age
(PubMed:15109498). {ECO:0000269|PubMed:15109498}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. S6 kinase subfamily. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; AY083469; AAM00022.1; -; mRNA.
EMBL; AL808146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS30502.1; -.
PIR; C32571; C32571.
PIR; S30504; S30504.
RefSeq; NP_683747.1; NM_148945.2.
PDB; 2QR7; X-ray; 2.00 A; A=399-740.
PDB; 2QR8; X-ray; 2.00 A; A=399-740.
PDB; 3G51; X-ray; 1.80 A; A=44-367.
PDB; 3UBD; X-ray; 1.53 A; A=45-346.
PDB; 4EL9; X-ray; 1.55 A; A=45-346.
PDB; 4GUE; X-ray; 1.80 A; A=45-346.
PDB; 4M8T; X-ray; 3.00 A; A=399-740.
PDB; 4MAO; X-ray; 2.60 A; A=399-740.
PDB; 5O1S; X-ray; 1.90 A; A=400-740.
PDBsum; 2QR7; -.
PDBsum; 2QR8; -.
PDBsum; 3G51; -.
PDBsum; 3UBD; -.
PDBsum; 4EL9; -.
PDBsum; 4GUE; -.
PDBsum; 4M8T; -.
PDBsum; 4MAO; -.
PDBsum; 5O1S; -.
SMR; P18654; -.
BioGRID; 225783; 14.
CORUM; P18654; -.
DIP; DIP-31554N; -.
ELM; P18654; -.
IntAct; P18654; 10.
MINT; P18654; -.
STRING; 10090.ENSMUSP00000033671; -.
BindingDB; P18654; -.
ChEMBL; CHEMBL3297641; -.
iPTMnet; P18654; -.
PhosphoSitePlus; P18654; -.
SwissPalm; P18654; -.
EPD; P18654; -.
jPOST; P18654; -.
MaxQB; P18654; -.
PaxDb; P18654; -.
PeptideAtlas; P18654; -.
PRIDE; P18654; -.
Antibodypedia; 1004; 582 antibodies.
DNASU; 110651; -.
Ensembl; ENSMUST00000033671; ENSMUSP00000033671; ENSMUSG00000031309.
GeneID; 110651; -.
KEGG; mmu:110651; -.
UCSC; uc009usj.2; mouse.
CTD; 6197; -.
MGI; MGI:104557; Rps6ka3.
eggNOG; KOG0603; Eukaryota.
GeneTree; ENSGT00940000159370; -.
InParanoid; P18654; -.
KO; K04373; -.
OrthoDB; 1132245at2759; -.
PhylomeDB; P18654; -.
TreeFam; TF313438; -.
Reactome; R-MMU-198753; ERK/MAPK targets.
Reactome; R-MMU-199920; CREB phosphorylation.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-442742; CREB1 phosphorylation through NMDA receptor-mediated activation of RAS signaling.
Reactome; R-MMU-444257; RSK activation.
Reactome; R-MMU-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
BioGRID-ORCS; 110651; 3 hits in 19 CRISPR screens.
ChiTaRS; Rps6ka3; mouse.
EvolutionaryTrace; P18654; -.
PRO; PR:P18654; -.
Proteomes; UP000000589; Chromosome X.
RNAct; P18654; protein.
Bgee; ENSMUSG00000031309; Expressed in trigeminal ganglion and 291 other tissues.
ExpressionAtlas; P18654; baseline and differential.
Genevisible; P18654; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:MGI.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0004711; F:ribosomal protein S6 kinase activity; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; IMP:UniProtKB.
CDD; cd14176; STKc_RSK2_C; 1.
CDD; cd05582; STKc_RSK_N; 1.
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; IPR016239; Ribosomal_S6_kinase_II.
InterPro; IPR041905; RPS6KA3_C.
InterPro; IPR041906; RSK_N.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 2.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 2.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell cycle; Cytoplasm; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Stress response; Transferase.
CHAIN 1..740
/note="Ribosomal protein S6 kinase alpha-3"
/id="PRO_0000086204"
DOMAIN 68..327
/note="Protein kinase 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
DOMAIN 328..397
/note="AGC-kinase C-terminal"
DOMAIN 422..679
/note="Protein kinase 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 74..82
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 428..436
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
ACT_SITE 193
/note="Proton acceptor"
/evidence="ECO:0000250"
ACT_SITE 539
/note="Proton acceptor"
/evidence="ECO:0000250"
BINDING 100
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 451
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 227
/note="Phosphoserine; by PDPK1"
/evidence="ECO:0000269|PubMed:10480933"
MOD_RES 365
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 369
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 375
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P51812"
MOD_RES 386
/note="Phosphoserine; by autocatalysis and MAPKAPK2"
/evidence="ECO:0000269|PubMed:10480933,
ECO:0000269|PubMed:17906627"
MOD_RES 415
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 529
/note="Phosphotyrosine; by FGFR3"
/evidence="ECO:0000269|PubMed:17785202"
MOD_RES 556
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P51812"
MOD_RES 715
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MUTAGEN 227
/note="S->E: Loss of phosphorylation and activation by
PDPK1."
/evidence="ECO:0000269|PubMed:10480933"
MUTAGEN 386
/note="S->A: Loss of phosphorylation by PDPK1; loss of
activation by PDPK1 and EGF."
/evidence="ECO:0000269|PubMed:10480933,
ECO:0000269|PubMed:10856237"
MUTAGEN 386
/note="S->E: Loss of interaction with PDPK1 and
phosphorylation at S-227."
/evidence="ECO:0000269|PubMed:10480933,
ECO:0000269|PubMed:10856237"
MUTAGEN 529
/note="Y->F: Attenuates activation by MAPK1/ERK1 and
MAPK3/ERK2."
/evidence="ECO:0000269|PubMed:17785202"
STRAND 50..56
/evidence="ECO:0000244|PDB:3UBD"
HELIX 65..67
/evidence="ECO:0000244|PDB:3UBD"
STRAND 68..75
/evidence="ECO:0000244|PDB:3UBD"
HELIX 77..79
/evidence="ECO:0000244|PDB:3UBD"
STRAND 81..87
/evidence="ECO:0000244|PDB:3UBD"
TURN 91..94
/evidence="ECO:0000244|PDB:3UBD"
STRAND 96..111
/evidence="ECO:0000244|PDB:3UBD"
HELIX 121..124
/evidence="ECO:0000244|PDB:3G51"
STRAND 133..139
/evidence="ECO:0000244|PDB:3UBD"
STRAND 142..147
/evidence="ECO:0000244|PDB:3UBD"
HELIX 156..162
/evidence="ECO:0000244|PDB:3UBD"
HELIX 167..186
/evidence="ECO:0000244|PDB:3UBD"
HELIX 196..198
/evidence="ECO:0000244|PDB:3UBD"
STRAND 199..201
/evidence="ECO:0000244|PDB:3UBD"
STRAND 207..216
/evidence="ECO:0000244|PDB:3UBD"
HELIX 232..234
/evidence="ECO:0000244|PDB:3UBD"
HELIX 237..241
/evidence="ECO:0000244|PDB:3UBD"
HELIX 248..263
/evidence="ECO:0000244|PDB:3UBD"
HELIX 273..282
/evidence="ECO:0000244|PDB:3UBD"
HELIX 293..302
/evidence="ECO:0000244|PDB:3UBD"
HELIX 307..309
/evidence="ECO:0000244|PDB:3UBD"
TURN 315..317
/evidence="ECO:0000244|PDB:3UBD"
HELIX 318..322
/evidence="ECO:0000244|PDB:3UBD"
HELIX 325..327
/evidence="ECO:0000244|PDB:3UBD"
HELIX 332..336
/evidence="ECO:0000244|PDB:3UBD"
HELIX 418..421
/evidence="ECO:0000244|PDB:5O1S"
STRAND 422..427
/evidence="ECO:0000244|PDB:5O1S"
STRAND 435..441
/evidence="ECO:0000244|PDB:5O1S"
TURN 442..444
/evidence="ECO:0000244|PDB:5O1S"
STRAND 447..454
/evidence="ECO:0000244|PDB:5O1S"
TURN 455..457
/evidence="ECO:0000244|PDB:5O1S"
HELIX 461..470
/evidence="ECO:0000244|PDB:5O1S"
STRAND 479..484
/evidence="ECO:0000244|PDB:5O1S"
STRAND 486..493
/evidence="ECO:0000244|PDB:5O1S"
STRAND 498..500
/evidence="ECO:0000244|PDB:4M8T"
HELIX 501..506
/evidence="ECO:0000244|PDB:5O1S"
HELIX 513..532
/evidence="ECO:0000244|PDB:5O1S"
HELIX 542..544
/evidence="ECO:0000244|PDB:5O1S"
STRAND 545..551
/evidence="ECO:0000244|PDB:5O1S"
HELIX 554..556
/evidence="ECO:0000244|PDB:5O1S"
STRAND 557..559
/evidence="ECO:0000244|PDB:5O1S"
HELIX 562..564
/evidence="ECO:0000244|PDB:4M8T"
HELIX 587..613
/evidence="ECO:0000244|PDB:5O1S"
STRAND 614..616
/evidence="ECO:0000244|PDB:5O1S"
STRAND 619..621
/evidence="ECO:0000244|PDB:5O1S"
HELIX 626..634
/evidence="ECO:0000244|PDB:5O1S"
HELIX 643..647
/evidence="ECO:0000244|PDB:5O1S"
HELIX 650..659
/evidence="ECO:0000244|PDB:5O1S"
TURN 664..666
/evidence="ECO:0000244|PDB:5O1S"
HELIX 670..673
/evidence="ECO:0000244|PDB:5O1S"
HELIX 677..680
/evidence="ECO:0000244|PDB:5O1S"
HELIX 682..684
/evidence="ECO:0000244|PDB:5O1S"
HELIX 696..711
/evidence="ECO:0000244|PDB:5O1S"
SEQUENCE 740 AA; 83694 MW; 0CD54E5918567007 CRC64;
MPLAQLADPW QKMAVESPSD SAENGQQIMD EPMGEEEINP QTEEGSIKEI AITHHVKEGH
EKADPSQFEL LKVLGQGSFG KVFLVKKISG SDARQLYAMK VLKKATLKVR DRVRTKMERD
ILVEVNHPFI VKLHYAFQTE GKLYLILDFL RGGDLFTRLS KEVMFTEEDV KFYLAELALA
LDHLHSLGII YRDLKPENIL LDEEGHIKLT DFGLSKESID HEKKAYSFCG TVEYMAPEVV
NRRGHTQSAD WWSFGVLMFE MLTGTLPFQG KDRKETMTMI LKAKLGMPQF LSPEAQSLLR
MLFKRNPANR LGAGPDGVEE IKRHSFFSTI DWNKLYRREI HPPFKPATGR PEDTFYFDPE
FTAKTPKDSP GIPPSANAHQ LFRGFSFVAI TSDDESQAMQ TVGVHSIVQQ LHRNSIQFTD
GYEVKEDIGV GSYSVCKRCI HKATNMEFAV KIIDKSKRDP TEEIEILLRY GQHPNIITLK
DVYDDGKYVY VVTELMKGGE LLDKILRQKF FSEREASAVL FTITKTVEYL HAQGVVHRDL
KPSNILYVDE SGNPESIRIC DFGFAKQLRA ENGLLMTPCY TANFVAPEVL KRQGYDAACD
IWSLGVLLYT MLTGYTPFAN GPDDTPEEIL ARIGSGKFSL SGGYWNSVSD TAKDLVSKML
HVDPHQRLTA ALVLRHPWIV HWDQLPQYQL NRQDAPHLVK GAMAATYSAL NRNQSPVLEP
VGRSTLAQRR GIKKITSTAL


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