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P18654

- KS6A3_MOUSE

UniProt

P18654 - KS6A3_MOUSE

Protein

Ribosomal protein S6 kinase alpha-3

Gene

Rps6ka3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (25 Mar 2003)
      Previous versions | rss
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    Functioni

    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. 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. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. 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. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). 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. 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. Phosphorylates DAPK1 By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei100 – 1001ATPPROSITE-ProRule annotation
    Active sitei193 – 1931Proton acceptorBy similarity
    Binding sitei451 – 4511ATPPROSITE-ProRule annotation
    Active sitei539 – 5391Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi74 – 829ATPPROSITE-ProRule annotation
    Nucleotide bindingi428 – 4369ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: Ensembl
    3. magnesium ion binding Source: InterPro
    4. protein kinase binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: MGI

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. intracellular signal transduction Source: InterPro
    3. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    4. response to lipopolysaccharide Source: UniProtKB
    5. response to stress Source: UniProtKB-KW
    6. toll-like receptor signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_198245. RSK activation.
    REACT_198246. CREB phosphorylation through the activation of Ras.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_215063. ERK/MAPK targets.
    REACT_224314. CREB phosphorylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal protein S6 kinase alpha-3 (EC:2.7.11.1)
    Short name:
    S6K-alpha-3
    Alternative name(s):
    90 kDa ribosomal protein S6 kinase 3
    Short name:
    p90-RSK 3
    Short name:
    p90RSK3
    MAP kinase-activated protein kinase 1b
    Short name:
    MAPK-activated protein kinase 1b
    Short name:
    MAPKAP kinase 1b
    Short name:
    MAPKAPK-1b
    Ribosomal S6 kinase 2
    Short name:
    RSK-2
    pp90RSK2
    Gene namesi
    Name:Rps6ka3
    Synonyms:Mapkapk1b, Rps6ka-rs1, Rsk2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:104557. Rps6ka3.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi227 – 2271S → E: Loss of phosphorylation and activation by PDPK1. 1 Publication
    Mutagenesisi386 – 3861S → A: Loss of phosphorylation by PDPK1; loss of activation by PDPK1 and EGF. 2 Publications
    Mutagenesisi386 – 3861S → E: Loss of interaction with PDPK1 and phosphorylation at S-227. 2 Publications
    Mutagenesisi529 – 5291Y → F: Attenuates activation by MAPK1/ERK1 and MAPK3/ERK2. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 740740Ribosomal protein S6 kinase alpha-3PRO_0000086204Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei227 – 2271Phosphoserine; by PDPK11 Publication
    Modified residuei365 – 3651PhosphothreonineBy similarity
    Modified residuei369 – 3691PhosphoserineBy similarity
    Modified residuei375 – 3751PhosphoserineBy similarity
    Modified residuei386 – 3861Phosphoserine; by autocatalysis and MAPKAPK22 Publications
    Modified residuei415 – 4151PhosphoserineBy similarity
    Modified residuei529 – 5291Phosphotyrosine; by FGFR31 Publication
    Modified residuei556 – 5561PhosphoserineBy similarity
    Modified residuei715 – 7151PhosphoserineBy similarity

    Post-translational modificationi

    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 MAPKAPK2.3 Publications
    N-terminal myristoylation results in an activated kinase in the absence of added growth factors.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP18654.
    PaxDbiP18654.
    PRIDEiP18654.

    PTM databases

    PhosphoSiteiP18654.

    Expressioni

    Tissue specificityi

    Intestine, thymus, lung, heart and brain.

    Gene expression databases

    ArrayExpressiP18654.
    BgeeiP18654.
    CleanExiMM_RPS6KA3.
    GenevestigatoriP18654.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi225783. 6 interactions.
    DIPiDIP-31554N.
    IntActiP18654. 7 interactions.
    MINTiMINT-1486771.

    Structurei

    Secondary structure

    1
    740
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 567
    Helixi65 – 673
    Beta strandi68 – 758
    Helixi77 – 793
    Beta strandi81 – 877
    Turni91 – 944
    Beta strandi96 – 11116
    Helixi121 – 1244
    Beta strandi133 – 1397
    Beta strandi142 – 1476
    Helixi156 – 1627
    Helixi167 – 18620
    Helixi196 – 1983
    Beta strandi199 – 2013
    Beta strandi207 – 21610
    Helixi232 – 2343
    Helixi237 – 2415
    Helixi248 – 26316
    Helixi273 – 28210
    Helixi293 – 30210
    Helixi307 – 3093
    Turni315 – 3173
    Helixi318 – 3225
    Helixi325 – 3273
    Helixi332 – 3365
    Helixi418 – 4214
    Beta strandi422 – 4309
    Beta strandi432 – 44110
    Turni442 – 4443
    Beta strandi447 – 4548
    Turni455 – 4573
    Helixi461 – 47010
    Beta strandi479 – 4846
    Beta strandi486 – 4938
    Helixi501 – 5066
    Helixi513 – 53220
    Helixi542 – 5443
    Beta strandi545 – 5517
    Helixi554 – 5563
    Beta strandi557 – 5593
    Helixi587 – 61327
    Helixi626 – 63510
    Turni643 – 6475
    Helixi650 – 65910
    Turni664 – 6663
    Helixi670 – 6734
    Helixi677 – 6804
    Helixi682 – 6843
    Helixi696 – 71015
    Turni711 – 7133

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QR7X-ray2.00A399-740[»]
    2QR8X-ray2.00A399-740[»]
    3G51X-ray1.80A44-367[»]
    3UBDX-ray1.53A45-346[»]
    4EL9X-ray1.55A45-346[»]
    4GUEX-ray1.80A45-346[»]
    ProteinModelPortaliP18654.
    SMRiP18654. Positions 51-714.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18654.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini68 – 327260Protein kinase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini328 – 39770AGC-kinase C-terminalAdd
    BLAST
    Domaini422 – 679258Protein kinase 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 2 protein kinase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110260.
    HOVERGENiHBG108317.
    InParanoidiB1AXN4.
    KOiK04373.
    OMAiHPWIVHC.
    PhylomeDBiP18654.
    TreeFamiTF313438.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR016239. Ribosomal_S6_kinase_II.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 2 hits.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000606. Ribsml_S6_kin_2. 1 hit.
    SMARTiSM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 2 hits.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 2 hits.
    PS50011. PROTEIN_KINASE_DOM. 2 hits.
    PS00108. PROTEIN_KINASE_ST. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P18654-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLAQLADPW QKMAVESPSD SAENGQQIMD EPMGEEEINP QTEEGSIKEI    50
    AITHHVKEGH EKADPSQFEL LKVLGQGSFG KVFLVKKISG SDARQLYAMK 100
    VLKKATLKVR DRVRTKMERD ILVEVNHPFI VKLHYAFQTE GKLYLILDFL 150
    RGGDLFTRLS KEVMFTEEDV KFYLAELALA LDHLHSLGII YRDLKPENIL 200
    LDEEGHIKLT DFGLSKESID HEKKAYSFCG TVEYMAPEVV NRRGHTQSAD 250
    WWSFGVLMFE MLTGTLPFQG KDRKETMTMI LKAKLGMPQF LSPEAQSLLR 300
    MLFKRNPANR LGAGPDGVEE IKRHSFFSTI DWNKLYRREI HPPFKPATGR 350
    PEDTFYFDPE FTAKTPKDSP GIPPSANAHQ LFRGFSFVAI TSDDESQAMQ 400
    TVGVHSIVQQ LHRNSIQFTD GYEVKEDIGV GSYSVCKRCI HKATNMEFAV 450
    KIIDKSKRDP TEEIEILLRY GQHPNIITLK DVYDDGKYVY VVTELMKGGE 500
    LLDKILRQKF FSEREASAVL FTITKTVEYL HAQGVVHRDL KPSNILYVDE 550
    SGNPESIRIC DFGFAKQLRA ENGLLMTPCY TANFVAPEVL KRQGYDAACD 600
    IWSLGVLLYT MLTGYTPFAN GPDDTPEEIL ARIGSGKFSL SGGYWNSVSD 650
    TAKDLVSKML HVDPHQRLTA ALVLRHPWIV HWDQLPQYQL NRQDAPHLVK 700
    GAMAATYSAL NRNQSPVLEP VGRSTLAQRR GIKKITSTAL 740
    Length:740
    Mass (Da):83,694
    Last modified:March 25, 2003 - v2
    Checksum:i0CD54E5918567007
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY083469 mRNA. Translation: AAM00022.1.
    AL808146 Genomic DNA. Translation: CAM25836.1.
    CCDSiCCDS30502.1.
    PIRiC32571.
    S30504.
    RefSeqiNP_683747.1. NM_148945.2.
    UniGeneiMm.328476.
    Mm.392829.

    Genome annotation databases

    EnsembliENSMUST00000033671; ENSMUSP00000033671; ENSMUSG00000031309.
    GeneIDi110651.
    KEGGimmu:110651.
    UCSCiuc009usj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY083469 mRNA. Translation: AAM00022.1 .
    AL808146 Genomic DNA. Translation: CAM25836.1 .
    CCDSi CCDS30502.1.
    PIRi C32571.
    S30504.
    RefSeqi NP_683747.1. NM_148945.2.
    UniGenei Mm.328476.
    Mm.392829.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QR7 X-ray 2.00 A 399-740 [» ]
    2QR8 X-ray 2.00 A 399-740 [» ]
    3G51 X-ray 1.80 A 44-367 [» ]
    3UBD X-ray 1.53 A 45-346 [» ]
    4EL9 X-ray 1.55 A 45-346 [» ]
    4GUE X-ray 1.80 A 45-346 [» ]
    ProteinModelPortali P18654.
    SMRi P18654. Positions 51-714.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 225783. 6 interactions.
    DIPi DIP-31554N.
    IntActi P18654. 7 interactions.
    MINTi MINT-1486771.

    Chemistry

    BindingDBi P18654.

    PTM databases

    PhosphoSitei P18654.

    Proteomic databases

    MaxQBi P18654.
    PaxDbi P18654.
    PRIDEi P18654.

    Protocols and materials databases

    DNASUi 110651.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033671 ; ENSMUSP00000033671 ; ENSMUSG00000031309 .
    GeneIDi 110651.
    KEGGi mmu:110651.
    UCSCi uc009usj.1. mouse.

    Organism-specific databases

    CTDi 6197.
    MGIi MGI:104557. Rps6ka3.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110260.
    HOVERGENi HBG108317.
    InParanoidi B1AXN4.
    KOi K04373.
    OMAi HPWIVHC.
    PhylomeDBi P18654.
    TreeFami TF313438.

    Enzyme and pathway databases

    Reactomei REACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_198245. RSK activation.
    REACT_198246. CREB phosphorylation through the activation of Ras.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_215063. ERK/MAPK targets.
    REACT_224314. CREB phosphorylation.

    Miscellaneous databases

    ChiTaRSi RPS6KA3. mouse.
    EvolutionaryTracei P18654.
    NextBioi 364399.
    PROi P18654.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P18654.
    Bgeei P18654.
    CleanExi MM_RPS6KA3.
    Genevestigatori P18654.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR016239. Ribosomal_S6_kinase_II.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 2 hits.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000606. Ribsml_S6_kin_2. 1 hit.
    SMARTi SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 2 hits.
    PS50011. PROTEIN_KINASE_DOM. 2 hits.
    PS00108. PROTEIN_KINASE_ST. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the p90 ribosomal S6 kinase 2 carboxyl-terminal domain as a protein kinase."
      Chrestensen C.A., Sturgill T.W.
      J. Biol. Chem. 277:27733-27741(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Sequence and expression of chicken and mouse rsk: homologs of Xenopus laevis ribosomal S6 kinase."
      Alcorta D.A., Crews C.M., Sweet L.J., Bankston L., Jones S.W., Erikson R.L.
      Mol. Cell. Biol. 9:3850-3859(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 108-740.
    4. "90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1."
      Jensen C.J., Buch M.-B., Krag T.O., Hemmings B.A., Gammeltoft S., Froedin M.
      J. Biol. Chem. 274:27168-27176(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-227 AND SER-386, MUTAGENESIS OF SER-227 AND SER-386.
    5. "A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1."
      Froedin M., Jensen C.J., Merienne K., Gammeltoft S.
      EMBO J. 19:2924-2934(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF SER-386.
    6. "Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6 kinases promotes its binding to 14-3-3 and cytoplasmic localization."
      Fujita N., Sato S., Tsuruo T.
      J. Biol. Chem. 278:49254-49260(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDKN1B.
    7. "FGFR3 activates RSK2 to mediate hematopoietic transformation through tyrosine phosphorylation of RSK2 and activation of the MEK/ERK pathway."
      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.
      Cancer Cell 12:201-214(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HEMATOPOIETIC TRANSFORMATION, PHOSPHORYLATION AT TYR-529, MUTAGENESIS OF TYR-529.
    8. "The MAPK-activated kinase Rsk controls an acute Toll-like receptor signaling response in dendritic cells and is activated through two distinct pathways."
      Zaru R., Ronkina N., Gaestel M., Arthur J.S., Watts C.
      Nat. Immunol. 8:1227-1235(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING, PHOSPHORYLATION AT SER-386.
    9. "Structural basis for activation of the autoinhibitory C-terminal kinase domain of p90 RSK2."
      Malakhova M., Tereshko V., Lee S.Y., Yao K., Cho Y.Y., Bode A., Dong Z.
      Nat. Struct. Mol. Biol. 15:112-113(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 399-740.
    10. "Structural diversity of the active N-terminal kinase domain of p90 ribosomal S6 kinase 2."
      Malakhova M., Kurinov I., Liu K., Zheng D., D'Angelo I., Shim J.H., Steinman V., Bode A.M., Dong Z.
      PLoS ONE 4:E8044-E8044(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 44-367.

    Entry informationi

    Entry nameiKS6A3_MOUSE
    AccessioniPrimary (citable) accession number: P18654
    Secondary accession number(s): B1AXN4, Q03140, Q8K3J8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: March 25, 2003
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3