KS6A3_MOUSE
ID KS6A3_MOUSE Reviewed; 740 AA.
AC P18654; B1AXN4; Q03140; Q8K3J8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Ribosomal protein S6 kinase alpha-3;
DE Short=S6K-alpha-3;
DE EC=2.7.11.1 {ECO:0000269|PubMed:15109498};
DE AltName: Full=90 kDa ribosomal protein S6 kinase 3;
DE Short=p90-RSK 3;
DE Short=p90RSK3;
DE AltName: Full=MAP kinase-activated protein kinase 1b;
DE Short=MAPK-activated protein kinase 1b;
DE Short=MAPKAP kinase 1b;
DE Short=MAPKAPK-1b;
DE AltName: Full=Ribosomal S6 kinase 2 {ECO:0000303|PubMed:15109498};
DE Short=RSK-2 {ECO:0000303|PubMed:15109498};
DE AltName: Full=pp90RSK2;
GN Name=Rps6ka3;
GN Synonyms=Mapkapk1b, Rps6ka-rs1, Rsk2 {ECO:0000303|PubMed:15109498};
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 [MRNA].
RX PubMed=12016217; DOI=10.1074/jbc.m202663200;
RA Chrestensen C.A., Sturgill T.W.;
RT "Characterization of the p90 ribosomal S6 kinase 2 carboxyl-terminal domain
RT as a protein kinase.";
RL J. Biol. Chem. 277:27733-27741(2002).
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 [MRNA] OF 108-740.
RX PubMed=2779569; DOI=10.1128/mcb.9.9.3850-3859.1989;
RA Alcorta D.A., Crews C.M., Sweet L.J., Bankston L., Jones S.W.,
RA Erikson R.L.;
RT "Sequence and expression of chicken and mouse rsk: homologs of Xenopus
RT laevis ribosomal S6 kinase.";
RL Mol. Cell. Biol. 9:3850-3859(1989).
RN [4]
RP ACTIVITY REGULATION, PHOSPHORYLATION AT SER-227 AND SER-386, AND
RP MUTAGENESIS OF SER-227 AND SER-386.
RX PubMed=10480933; DOI=10.1074/jbc.274.38.27168;
RA Jensen C.J., Buch M.-B., Krag T.O., Hemmings B.A., Gammeltoft S.,
RA Froedin M.;
RT "90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-
RT phosphoinositide-dependent protein kinase-1.";
RL J. Biol. Chem. 274:27168-27176(1999).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF SER-386.
RX PubMed=10856237; DOI=10.1093/emboj/19.12.2924;
RA Froedin M., Jensen C.J., Merienne K., Gammeltoft S.;
RT "A phosphoserine-regulated docking site in the protein kinase RSK2 that
RT recruits and activates PDK1.";
RL EMBO J. 19:2924-2934(2000).
RN [6]
RP FUNCTION IN PHOSPHORYLATION OF CDKN1B.
RX PubMed=14504289; DOI=10.1074/jbc.m306614200;
RA Fujita N., Sato S., Tsuruo T.;
RT "Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6
RT kinases promotes its binding to 14-3-3 and cytoplasmic localization.";
RL J. Biol. Chem. 278:49254-49260(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15109498; DOI=10.1016/s0092-8674(04)00344-7;
RA Yang X., Matsuda K., Bialek P., Jacquot S., Masuoka H.C., Schinke T.,
RA Li L., Brancorsini S., Sassone-Corsi P., Townes T.M., Hanauer A.,
RA Karsenty G.;
RT "ATF4 is a substrate of RSK2 and an essential regulator of osteoblast
RT biology; implication for Coffin-Lowry Syndrome.";
RL Cell 117:387-398(2004).
RN [8]
RP FUNCTION IN HEMATOPOIETIC TRANSFORMATION, PHOSPHORYLATION AT TYR-529, AND
RP MUTAGENESIS OF TYR-529.
RX PubMed=17785202; DOI=10.1016/j.ccr.2007.08.003;
RA Kang S., Dong S., Gu T.L., Guo A., Cohen M.S., Lonial S., Khoury H.J.,
RA Fabbro D., Gilliland D.G., Bergsagel P.L., Taunton J., Polakiewicz R.D.,
RA Chen J.;
RT "FGFR3 activates RSK2 to mediate hematopoietic transformation through
RT tyrosine phosphorylation of RSK2 and activation of the MEK/ERK pathway.";
RL Cancer Cell 12:201-214(2007).
RN [9]
RP FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING, AND PHOSPHORYLATION AT SER-386.
RX PubMed=17906627; DOI=10.1038/ni1517;
RA Zaru R., Ronkina N., Gaestel M., Arthur J.S., Watts C.;
RT "The MAPK-activated kinase Rsk controls an acute Toll-like receptor
RT signaling response in dendritic cells and is activated through two distinct
RT pathways.";
RL Nat. Immunol. 8:1227-1235(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369; SER-415 AND
RP SER-715, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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 [11]
RP FUNCTION.
RX PubMed=22827337; DOI=10.1042/bj20120938;
RA Saha M., Carriere A., Cheerathodi M., Zhang X., Lavoie G., Rush J.,
RA Roux P.P., Ballif B.A.;
RT "RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively
RT regulating MAPK activation.";
RL Biochem. J. 447:159-166(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 399-740.
RX PubMed=18084304; DOI=10.1038/nsmb1347;
RA Malakhova M., Tereshko V., Lee S.Y., Yao K., Cho Y.Y., Bode A., Dong Z.;
RT "Structural basis for activation of the autoinhibitory C-terminal kinase
RT domain of p90 RSK2.";
RL Nat. Struct. Mol. Biol. 15:112-113(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 44-367.
RX PubMed=19956600; DOI=10.1371/journal.pone.0008044;
RA Malakhova M., Kurinov I., Liu K., Zheng D., D'Angelo I., Shim J.H.,
RA Steinman V., Bode A.M., Dong Z.;
RT "Structural diversity of the active N-terminal kinase domain of p90
RT ribosomal S6 kinase 2.";
RL PLoS ONE 4:E8044-E8044(2009).
CC -!- FUNCTION: Serine/threonine-protein kinase that acts downstream of ERK
CC (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and
CC stress-induced activation of the transcription factors CREB1, ETV1/ER81
CC and NR4A1/NUR77, regulates translation through RPS6 and EIF4B
CC phosphorylation, and mediates cellular proliferation, survival, and
CC differentiation by modulating mTOR signaling and repressing pro-
CC apoptotic function of BAD and DAPK1 (PubMed:10856237, PubMed:15109498).
CC In fibroblast, is required for EGF-stimulated phosphorylation of CREB1
CC and histone H3 at 'Ser-10', which results in the subsequent
CC transcriptional activation of several immediate-early genes (By
CC similarity). In response to mitogenic stimulation (EGF and PMA),
CC phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription
CC factors and the cofactor CREBBP (By similarity). Upon insulin-derived
CC signal, acts indirectly on the transcription regulation of several
CC genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity
CC (By similarity). Phosphorylates RPS6 in response to serum or EGF via an
CC mTOR-independent mechanism and promotes translation initiation by
CC facilitating assembly of the preinitiation complex (By similarity). In
CC response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for
CC the EIF3 complex and stimulating cap-dependent translation (By
CC similarity). Is involved in the mTOR nutrient-sensing pathway by
CC directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits
CC TSC2 ability to suppress mTOR signaling, and mediates phosphorylation
CC of RPTOR, which regulates mTORC1 activity and may promote rapamycin-
CC sensitive signaling independently of the PI3K/AKT pathway (By
CC similarity). Mediates cell survival by phosphorylating the pro-
CC apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic
CC function (By similarity). Promotes the survival of hepatic stellate
CC cells by phosphorylating CEBPB in response to the hepatotoxin carbon
CC tetrachloride (CCl4) (By similarity). Is involved in cell cycle
CC regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes
CC CDKN1B association with 14-3-3 proteins and prevents its translocation
CC to the nucleus and inhibition of G1 progression (PubMed:14504289). In
CC LPS-stimulated dendritic cells, is involved in TLR4-induced
CC macropinocytosis, and in myeloma cells, acts as effector of FGFR3-
CC mediated transformation signaling, after direct phosphorylation at Tyr-
CC 529 by FGFR3 (PubMed:17785202, PubMed:17906627). Negatively regulates
CC EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1
CC (PubMed:22827337). Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161'
CC that create YWHAB and YWHAE binding sites and which contribute to the
CC negative regulation of MAPK1/3 phosphorylation (PubMed:22827337).
CC Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway
CC controls cell migration (By similarity). Acts as a regulator of
CC osteoblast differentiation by mediating phosphorylation of ATF4,
CC thereby promoting ATF4 transactivation activity (PubMed:15109498).
CC {ECO:0000250|UniProtKB:P51812, ECO:0000269|PubMed:10856237,
CC ECO:0000269|PubMed:14504289, ECO:0000269|PubMed:15109498,
CC ECO:0000269|PubMed:17785202, ECO:0000269|PubMed:17906627,
CC ECO:0000269|PubMed:22827337}.
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:15109498};
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Upon extracellular signal or mitogen stimulation,
CC phosphorylated at Thr-577 in the C-terminal kinase domain (CTKD) by
CC MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates
CC Ser-386, allowing binding of PDPK1, which in turn phosphorylates Ser-
CC 227 in the N-terminal kinase domain (NTDK) leading to the full
CC activation of the protein and subsequent phosphorylation of the
CC substrates by the NTKD (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in
CC quiescent cells. Transiently dissociates following mitogenic
CC stimulation (By similarity). Interacts with NFATC4, ETV1/ER81 and FGFR1
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P18654; P30309: cdc25-1-b; Xeno; NbExp=3; IntAct=EBI-397744, EBI-15888737;
CC P18654; P28223-1: HTR2A; Xeno; NbExp=2; IntAct=EBI-397744, EBI-15573967;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51812}. Cytoplasm
CC {ECO:0000250|UniProtKB:P51812}.
CC -!- TISSUE SPECIFICITY: Intestine, thymus, lung, heart and brain.
CC -!- PTM: Activated by phosphorylation at Ser-227 by PDPK1.
CC Autophosphorylated on Ser-386, as part of the activation process. May
CC be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and MAPK3/ERK1.
CC Can also be activated via phosphorylation at Ser-386 by MAPKAPK2.
CC {ECO:0000269|PubMed:10480933, ECO:0000269|PubMed:17785202,
CC ECO:0000269|PubMed:17906627}.
CC -!- PTM: N-terminal myristoylation results in an activated kinase in the
CC absence of added growth factors. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice were born at expected Mendelian ratio but
CC display decreased bone mass (PubMed:15109498). Embryos and pups show a
CC delay in mineralization of the skull with frontal, parietal, and
CC interparietal bones of reduced size (PubMed:15109498). Mice also
CC display a significant reduction in long bone length at one month of age
CC (PubMed:15109498). {ECO:0000269|PubMed:15109498}.
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; AY083469; AAM00022.1; -; mRNA.
DR EMBL; AL808146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30502.1; -.
DR PIR; C32571; C32571.
DR PIR; S30504; S30504.
DR RefSeq; NP_683747.1; NM_148945.2.
DR PDB; 2QR7; X-ray; 2.00 A; A=399-740.
DR PDB; 2QR8; X-ray; 2.00 A; A=399-740.
DR PDB; 3G51; X-ray; 1.80 A; A=44-367.
DR PDB; 3UBD; X-ray; 1.53 A; A=45-346.
DR PDB; 4EL9; X-ray; 1.55 A; A=45-346.
DR PDB; 4GUE; X-ray; 1.80 A; A=45-346.
DR PDB; 4M8T; X-ray; 3.00 A; A=399-740.
DR PDB; 4MAO; X-ray; 2.60 A; A=399-740.
DR PDB; 5O1S; X-ray; 1.90 A; A=400-740.
DR PDBsum; 2QR7; -.
DR PDBsum; 2QR8; -.
DR PDBsum; 3G51; -.
DR PDBsum; 3UBD; -.
DR PDBsum; 4EL9; -.
DR PDBsum; 4GUE; -.
DR PDBsum; 4M8T; -.
DR PDBsum; 4MAO; -.
DR PDBsum; 5O1S; -.
DR AlphaFoldDB; P18654; -.
DR SMR; P18654; -.
DR BioGRID; 225783; 14.
DR CORUM; P18654; -.
DR DIP; DIP-31554N; -.
DR ELM; P18654; -.
DR IntAct; P18654; 8.
DR MINT; P18654; -.
DR STRING; 10090.ENSMUSP00000033671; -.
DR BindingDB; P18654; -.
DR ChEMBL; CHEMBL3297641; -.
DR iPTMnet; P18654; -.
DR PhosphoSitePlus; P18654; -.
DR SwissPalm; P18654; -.
DR EPD; P18654; -.
DR jPOST; P18654; -.
DR MaxQB; P18654; -.
DR PaxDb; P18654; -.
DR PeptideAtlas; P18654; -.
DR PRIDE; P18654; -.
DR ProteomicsDB; 265029; -.
DR Antibodypedia; 1004; 612 antibodies from 36 providers.
DR DNASU; 110651; -.
DR Ensembl; ENSMUST00000033671; ENSMUSP00000033671; ENSMUSG00000031309.
DR GeneID; 110651; -.
DR KEGG; mmu:110651; -.
DR UCSC; uc009usj.2; mouse.
DR CTD; 6197; -.
DR MGI; MGI:104557; Rps6ka3.
DR VEuPathDB; HostDB:ENSMUSG00000031309; -.
DR eggNOG; KOG0603; Eukaryota.
DR GeneTree; ENSGT00940000159370; -.
DR InParanoid; P18654; -.
DR OMA; VINCCEA; -.
DR OrthoDB; 1132245at2759; -.
DR PhylomeDB; P18654; -.
DR TreeFam; TF313438; -.
DR BioGRID-ORCS; 110651; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Rps6ka3; mouse.
DR EvolutionaryTrace; P18654; -.
DR PRO; PR:P18654; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P18654; protein.
DR Bgee; ENSMUSG00000031309; Expressed in trigeminal ganglion and 254 other tissues.
DR ExpressionAtlas; P18654; baseline and differential.
DR Genevisible; P18654; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0004711; F:ribosomal protein S6 kinase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IMP:UniProtKB.
DR CDD; cd14176; STKc_RSK2_C; 1.
DR CDD; cd05582; STKc_RSK_N; 1.
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; IPR016239; Ribosomal_S6_kinase_II.
DR InterPro; IPR041905; RPS6KA3_C.
DR InterPro; IPR041906; RSK_N.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT CHAIN 1..740
FT /note="Ribosomal protein S6 kinase alpha-3"
FT /id="PRO_0000086204"
FT DOMAIN 68..327
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 328..397
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 422..679
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 539
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 74..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 428..436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 227
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000269|PubMed:10480933"
FT MOD_RES 365
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51812"
FT MOD_RES 386
FT /note="Phosphoserine; by autocatalysis and MAPKAPK2"
FT /evidence="ECO:0000269|PubMed:10480933,
FT ECO:0000269|PubMed:17906627"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 529
FT /note="Phosphotyrosine; by FGFR3"
FT /evidence="ECO:0000269|PubMed:17785202"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51812"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 227
FT /note="S->E: Loss of phosphorylation and activation by
FT PDPK1."
FT /evidence="ECO:0000269|PubMed:10480933"
FT MUTAGEN 386
FT /note="S->A: Loss of phosphorylation by PDPK1; loss of
FT activation by PDPK1 and EGF."
FT /evidence="ECO:0000269|PubMed:10480933,
FT ECO:0000269|PubMed:10856237"
FT MUTAGEN 386
FT /note="S->E: Loss of interaction with PDPK1 and
FT phosphorylation at S-227."
FT /evidence="ECO:0000269|PubMed:10480933,
FT ECO:0000269|PubMed:10856237"
FT MUTAGEN 529
FT /note="Y->F: Attenuates activation by MAPK1/ERK1 and
FT MAPK3/ERK2."
FT /evidence="ECO:0000269|PubMed:17785202"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3UBD"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3UBD"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:3UBD"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:3UBD"
FT STRAND 96..111
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:3G51"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:3UBD"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3UBD"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3UBD"
FT STRAND 207..216
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 248..263
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:3UBD"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:3UBD"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:5O1S"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:5O1S"
FT STRAND 435..441
FT /evidence="ECO:0007829|PDB:5O1S"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:5O1S"
FT STRAND 447..454
FT /evidence="ECO:0007829|PDB:5O1S"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 461..470
FT /evidence="ECO:0007829|PDB:5O1S"
FT STRAND 479..484
FT /evidence="ECO:0007829|PDB:5O1S"
FT STRAND 486..493
FT /evidence="ECO:0007829|PDB:5O1S"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:4M8T"
FT HELIX 501..506
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 513..532
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:5O1S"
FT STRAND 545..551
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:5O1S"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:4M8T"
FT HELIX 587..613
FT /evidence="ECO:0007829|PDB:5O1S"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:5O1S"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 626..634
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 643..647
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 650..659
FT /evidence="ECO:0007829|PDB:5O1S"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 670..673
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 677..680
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 682..684
FT /evidence="ECO:0007829|PDB:5O1S"
FT HELIX 696..711
FT /evidence="ECO:0007829|PDB:5O1S"
SQ 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
