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P51812

- KS6A3_HUMAN

UniProt

P51812 - KS6A3_HUMAN

Protein

Ribosomal protein S6 kinase alpha-3

Gene

RPS6KA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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 DAPK1.7 Publications

    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.

    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: UniProtKB
    3. magnesium ion binding Source: InterPro
    4. protein kinase activity Source: ProtInc
    5. protein serine/threonine kinase activity Source: ProtInc

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell cycle Source: UniProtKB-KW
    3. central nervous system development Source: ProtInc
    4. innate immune response Source: Reactome
    5. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    6. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    7. negative regulation of apoptotic process Source: UniProtKB
    8. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    9. neurotrophin TRK receptor signaling pathway Source: Reactome
    10. positive regulation of cell differentiation Source: UniProtKB
    11. positive regulation of cell growth Source: UniProtKB
    12. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    13. regulation of DNA-templated transcription in response to stress Source: UniProtKB
    14. regulation of translation in response to stress Source: UniProtKB
    15. response to lipopolysaccharide Source: UniProtKB
    16. signal transduction Source: ProtInc
    17. skeletal system development Source: ProtInc
    18. stress-activated MAPK cascade Source: Reactome
    19. synaptic transmission Source: Reactome
    20. toll-like receptor 10 signaling pathway Source: Reactome
    21. toll-like receptor 2 signaling pathway Source: Reactome
    22. toll-like receptor 3 signaling pathway Source: Reactome
    23. toll-like receptor 4 signaling pathway Source: Reactome
    24. toll-like receptor 5 signaling pathway Source: Reactome
    25. toll-like receptor 9 signaling pathway Source: Reactome
    26. toll-like receptor signaling pathway Source: UniProtKB
    27. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    28. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    29. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Stress response

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_12524. CREB phosphorylation.
    REACT_12599. ERK/MAPK targets.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_20510. RSK activation.
    REACT_20568. CREB phosphorylation through the activation of Ras.
    REACT_22365. Recycling pathway of L1.
    SignaLinkiP51812.

    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
    Insulin-stimulated protein kinase 1
    Short name:
    ISPK-1
    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:ISPK1, MAPKAPK1B, RSK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:10432. RPS6KA3.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Coffin-Lowry syndrome (CLS) [MIM:303600]: A X-linked mental retardation associated with facial and digital dysmorphisms, progressive skeletal malformations, growth retardation, hearing deficit and paroxysmal movement disorders.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti75 – 751G → V in CLS. 1 Publication
    VAR_006189
    Natural varianti82 – 821V → F in CLS. 1 Publication
    VAR_006190
    Natural varianti114 – 1141R → W in CLS. 1 Publication
    VAR_006191
    Natural varianti127 – 1271H → Q in CLS. 1 Publication
    VAR_006192
    Natural varianti154 – 1541D → Y in CLS. 1 Publication
    VAR_006193
    Natural varianti189 – 1891I → K in CLS. 1 Publication
    VAR_065894
    Natural varianti225 – 2251A → V in CLS. 1 Publication
    VAR_006194
    Natural varianti227 – 2271S → A in CLS. 1 Publication
    VAR_006195
    Natural varianti268 – 2681F → S in CLS. 1 Publication
    VAR_065896
    Natural varianti431 – 4311G → D in CLS. 1 Publication
    VAR_006196
    Natural varianti477 – 4771Missing in CLS. 1 Publication
    VAR_065898
    Natural varianti729 – 7291R → Q in CLS. 1 Publication
    Corresponds to variant rs28935171 [ dbSNP | Ensembl ].
    VAR_006197
    Mental retardation, X-linked 19 (MRX19) [MIM:300844]: A non-syndromic form of mild to moderate mental retardation. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. In contrast to syndromic or specific X-linked mental retardation which also present with associated physical, neurological and/or psychiatric manifestations, intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti115 – 1151T → S in MRX19. 1 Publication
    VAR_065892
    Natural varianti152 – 1521Missing in MRX19. 1 Publication
    VAR_065893
    Natural varianti202 – 2021Missing in MRX19. 1 Publication
    VAR_065895
    Natural varianti383 – 3831R → W in MRX19; kinase activity is decreased but not abolished. 1 Publication
    VAR_065897

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi300844. phenotype.
    303600. phenotype.
    Orphaneti192. Coffin-Lowry syndrome.
    777. X-linked non-syndromic intellectual disability.
    PharmGKBiPA34847.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 740740Ribosomal protein S6 kinase alpha-3PRO_0000086203Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei227 – 2271Phosphoserine; by PDPK1Curated
    Modified residuei365 – 3651Phosphothreonine4 Publications
    Modified residuei369 – 3691Phosphoserine4 Publications
    Modified residuei375 – 3751Phosphoserine3 Publications
    Modified residuei386 – 3861Phosphoserine; by autocatalysis and MAPKAPK22 Publications
    Modified residuei415 – 4151Phosphoserine3 Publications
    Modified residuei529 – 5291Phosphotyrosine; by FGFR3By similarity
    Modified residuei556 – 5561Phosphoserine1 Publication
    Modified residuei715 – 7151Phosphoserine4 Publications

    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 MAPKAPK2.7 Publications
    N-terminal myristoylation results in an activated kinase in the absence of added growth factors.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP51812.
    PaxDbiP51812.
    PeptideAtlasiP51812.
    PRIDEiP51812.

    PTM databases

    PhosphoSiteiP51812.

    Expressioni

    Tissue specificityi

    Expressed in many tissues, highest levels in skeletal muscle.

    Gene expression databases

    ArrayExpressiP51812.
    BgeeiP51812.
    CleanExiHS_RPS6KA3.
    GenevestigatoriP51812.

    Organism-specific databases

    HPAiCAB003853.
    CAB013520.
    HPA003221.

    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 similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAPK1P284823EBI-1046616,EBI-959949

    Protein-protein interaction databases

    BioGridi112111. 35 interactions.
    DIPiDIP-38247N.
    IntActiP51812. 14 interactions.
    MINTiMINT-1542962.
    STRINGi9606.ENSP00000368884.

    Structurei

    Secondary structure

    1
    740
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi65 – 673
    Beta strandi68 – 769
    Beta strandi78 – 8710
    Turni91 – 944
    Beta strandi96 – 1049
    Turni105 – 1073
    Helixi109 – 12416
    Beta strandi133 – 1397
    Beta strandi142 – 1487
    Helixi155 – 1628
    Helixi167 – 18620
    Beta strandi189 – 1924
    Helixi196 – 1983
    Beta strandi199 – 2013
    Beta strandi203 – 2053
    Beta strandi207 – 2093
    Beta strandi214 – 2163
    Helixi217 – 2237
    Turni224 – 2263
    Helixi232 – 2343
    Helixi237 – 2404
    Helixi249 – 26315
    Helixi273 – 28210
    Helixi293 – 30210
    Helixi307 – 3093
    Turni315 – 3184
    Helixi319 – 3224
    Helixi325 – 3273
    Helixi332 – 3365
    Beta strandi409 – 4113
    Helixi412 – 4143
    Turni419 – 4213
    Beta strandi422 – 4309
    Beta strandi432 – 44110
    Turni442 – 4454
    Beta strandi446 – 4549
    Turni455 – 4573
    Helixi461 – 47010
    Beta strandi479 – 4846
    Beta strandi486 – 4949
    Helixi501 – 5066
    Helixi513 – 53220
    Helixi542 – 5443
    Beta strandi545 – 5517
    Helixi554 – 5563
    Beta strandi557 – 5593
    Beta strandi571 – 5733
    Helixi587 – 61327
    Helixi626 – 63510
    Helixi643 – 6453
    Beta strandi646 – 6483
    Helixi650 – 65910
    Turni664 – 6663
    Helixi670 – 6734
    Helixi677 – 6804
    Helixi682 – 6843
    Helixi696 – 71015
    Helixi711 – 7133

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4D9TX-ray2.40A399-740[»]
    4D9UX-ray2.40A399-740[»]
    4JG6X-ray2.60A399-740[»]
    4JG7X-ray3.00A399-740[»]
    4JG8X-ray3.10A399-740[»]
    4NUSX-ray2.39A39-359[»]
    4NW5X-ray1.94A39-359[»]
    4NW6X-ray1.74A39-359[»]
    ProteinModelPortaliP51812.
    SMRiP51812. Positions 51-714.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiP51812.
    KOiK04373.
    OMAiHPWIVHC.
    OrthoDBiEOG7B8S38.
    PhylomeDBiP51812.
    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.

    P51812-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLAQLADPW QKMAVESPSD SAENGQQIMD EPMGEEEINP QTEEVSIKEI    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):83,736
    Last modified:October 1, 1996 - v1
    Checksum:i486AE8357CEAB6C8
    GO

    Sequence cautioni

    The sequence BAD92170.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891S → L in AAH96303. (PubMed:15489334)Curated
    Sequence conflicti410 – 4101Missing in BAD92170. 1 PublicationCurated
    Sequence conflicti424 – 4241V → L in AAC82495. (PubMed:8141249)Curated
    Sequence conflicti480 – 4801K → N in AAC82495. (PubMed:8141249)Curated
    Sequence conflicti494 – 4941Missing in AAC82495. (PubMed:8141249)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381I → S.2 Publications
    Corresponds to variant rs56218010 [ dbSNP | Ensembl ].
    VAR_006188
    Natural varianti75 – 751G → V in CLS. 1 Publication
    VAR_006189
    Natural varianti82 – 821V → F in CLS. 1 Publication
    VAR_006190
    Natural varianti114 – 1141R → W in CLS. 1 Publication
    VAR_006191
    Natural varianti115 – 1151T → S in MRX19. 1 Publication
    VAR_065892
    Natural varianti127 – 1271H → Q in CLS. 1 Publication
    VAR_006192
    Natural varianti152 – 1521Missing in MRX19. 1 Publication
    VAR_065893
    Natural varianti154 – 1541D → Y in CLS. 1 Publication
    VAR_006193
    Natural varianti189 – 1891I → K in CLS. 1 Publication
    VAR_065894
    Natural varianti202 – 2021Missing in MRX19. 1 Publication
    VAR_065895
    Natural varianti225 – 2251A → V in CLS. 1 Publication
    VAR_006194
    Natural varianti227 – 2271S → A in CLS. 1 Publication
    VAR_006195
    Natural varianti268 – 2681F → S in CLS. 1 Publication
    VAR_065896
    Natural varianti383 – 3831R → W in MRX19; kinase activity is decreased but not abolished. 1 Publication
    VAR_065897
    Natural varianti416 – 4161I → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035627
    Natural varianti431 – 4311G → D in CLS. 1 Publication
    VAR_006196
    Natural varianti477 – 4771Missing in CLS. 1 Publication
    VAR_065898
    Natural varianti483 – 4831Y → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040629
    Natural varianti608 – 6081L → F in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_040630
    Natural varianti723 – 7231R → C.1 Publication
    Corresponds to variant rs35026425 [ dbSNP | Ensembl ].
    VAR_040631
    Natural varianti729 – 7291R → Q in CLS. 1 Publication
    Corresponds to variant rs28935171 [ dbSNP | Ensembl ].
    VAR_006197

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08316 mRNA. Translation: AAA81952.1.
    AK313932 mRNA. Translation: BAG36651.1.
    AB208933 mRNA. Translation: BAD92170.1. Different initiation.
    AL732366, AL807772 Genomic DNA. Translation: CAI40548.1.
    AL807772, AL732366 Genomic DNA. Translation: CAI39687.1.
    BC096301 mRNA. Translation: AAH96301.1.
    BC096302 mRNA. Translation: AAH96302.1.
    BC096303 mRNA. Translation: AAH96303.1.
    L07599 mRNA. Translation: AAC82495.1.
    AB102662 mRNA. Translation: BAC81131.1.
    CCDSiCCDS14197.1.
    PIRiI38556.
    RefSeqiNP_004577.1. NM_004586.2.
    UniGeneiHs.445387.

    Genome annotation databases

    EnsembliENST00000379565; ENSP00000368884; ENSG00000177189.
    GeneIDi6197.
    KEGGihsa:6197.
    UCSCiuc004czu.3. human.

    Polymorphism databases

    DMDMi1730070.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08316 mRNA. Translation: AAA81952.1 .
    AK313932 mRNA. Translation: BAG36651.1 .
    AB208933 mRNA. Translation: BAD92170.1 . Different initiation.
    AL732366 , AL807772 Genomic DNA. Translation: CAI40548.1 .
    AL807772 , AL732366 Genomic DNA. Translation: CAI39687.1 .
    BC096301 mRNA. Translation: AAH96301.1 .
    BC096302 mRNA. Translation: AAH96302.1 .
    BC096303 mRNA. Translation: AAH96303.1 .
    L07599 mRNA. Translation: AAC82495.1 .
    AB102662 mRNA. Translation: BAC81131.1 .
    CCDSi CCDS14197.1.
    PIRi I38556.
    RefSeqi NP_004577.1. NM_004586.2.
    UniGenei Hs.445387.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4D9T X-ray 2.40 A 399-740 [» ]
    4D9U X-ray 2.40 A 399-740 [» ]
    4JG6 X-ray 2.60 A 399-740 [» ]
    4JG7 X-ray 3.00 A 399-740 [» ]
    4JG8 X-ray 3.10 A 399-740 [» ]
    4NUS X-ray 2.39 A 39-359 [» ]
    4NW5 X-ray 1.94 A 39-359 [» ]
    4NW6 X-ray 1.74 A 39-359 [» ]
    ProteinModelPortali P51812.
    SMRi P51812. Positions 51-714.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112111. 35 interactions.
    DIPi DIP-38247N.
    IntActi P51812. 14 interactions.
    MINTi MINT-1542962.
    STRINGi 9606.ENSP00000368884.

    Chemistry

    BindingDBi P51812.
    ChEMBLi CHEMBL2345.
    GuidetoPHARMACOLOGYi 1528.

    PTM databases

    PhosphoSitei P51812.

    Polymorphism databases

    DMDMi 1730070.

    Proteomic databases

    MaxQBi P51812.
    PaxDbi P51812.
    PeptideAtlasi P51812.
    PRIDEi P51812.

    Protocols and materials databases

    DNASUi 6197.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379565 ; ENSP00000368884 ; ENSG00000177189 .
    GeneIDi 6197.
    KEGGi hsa:6197.
    UCSCi uc004czu.3. human.

    Organism-specific databases

    CTDi 6197.
    GeneCardsi GC0XM020168.
    GeneReviewsi RPS6KA3.
    HGNCi HGNC:10432. RPS6KA3.
    HPAi CAB003853.
    CAB013520.
    HPA003221.
    MIMi 300075. gene.
    300844. phenotype.
    303600. phenotype.
    neXtProti NX_P51812.
    Orphaneti 192. Coffin-Lowry syndrome.
    777. X-linked non-syndromic intellectual disability.
    PharmGKBi PA34847.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi P51812.
    KOi K04373.
    OMAi HPWIVHC.
    OrthoDBi EOG7B8S38.
    PhylomeDBi P51812.
    TreeFami TF313438.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_12524. CREB phosphorylation.
    REACT_12599. ERK/MAPK targets.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_20510. RSK activation.
    REACT_20568. CREB phosphorylation through the activation of Ras.
    REACT_22365. Recycling pathway of L1.
    SignaLinki P51812.

    Miscellaneous databases

    ChiTaRSi RPS6KA3. human.
    GeneWikii RPS6KA3.
    GenomeRNAii 6197.
    NextBioi 24069.
    PROi P51812.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51812.
    Bgeei P51812.
    CleanExi HS_RPS6KA3.
    Genevestigatori P51812.

    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. "Cloning of a human insulin-stimulated protein kinase (ISPK-1) gene and analysis of coding regions and mRNA levels of the ISPK-1 and the protein phosphatase-1 genes in muscle from NIDDM patients."
      Bjoerbaek C., Vik T.A., Echwald S.M., Webb G.C., Wang J.P., Yang P.-Y., Vestergaard H., Richmond K., Hansen T., Erikson R.L., Miklos G.L.G., Cohen P.T.W., Pedersen O.
      Diabetes 44:90-97(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta and T-cell.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Human rsk isoforms: cloning and characterization of tissue-specific expression."
      Moller D.E., Xia C.-H., Tang W., Zhu A.X., Jakubowski M.
      Am. J. Physiol. 266:C351-C359(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-582.
      Tissue: Skeletal muscle.
    7. "Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees."
      Kitano T., Schwarz C., Nickel B., Paeaebo S.
      Mol. Biol. Evol. 20:1281-1289(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-735.
    8. "Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling."
      Sutherland C., Leighton I.A., Cohen P.
      Biochem. J. 296:15-19(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF GSK3B.
    9. "Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene."
      De Cesare D., Jacquot S., Hanauer A., Sassone-Corsi P.
      Proc. Natl. Acad. Sci. U.S.A. 95:12202-12207(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1.
    10. "Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3."
      Sassone-Corsi P., Mizzen C.A., Cheung P., Crosio C., Monaco L., Jacquot S., Hanauer A., Allis C.D.
      Science 285:886-891(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
    11. "The tumor suppressor DAP kinase is a target of RSK-mediated survival signaling."
      Anjum R., Roux P.P., Ballif B.A., Gygi S.P., Blenis J.
      Curr. Biol. 15:1762-1767(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF DAPK1.
    12. "Nur77 is phosphorylated in cells by RSK in response to mitogenic stimulation."
      Wingate A.D., Campbell D.G., Peggie M., Arthur J.S.
      Biochem. J. 393:715-724(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF NR4A1/NUR77.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: INTERACTION WITH NFATC4.
    15. "RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation."
      Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J., Sonenberg N., Blenis J.
      J. Biol. Chem. 282:14056-14064(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6.
    16. "Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-mediated raptor phosphorylation."
      Carriere A., Cargnello M., Julien L.A., Gao H., Bonneil E., Thibault P., Roux P.P.
      Curr. Biol. 18:1269-1277(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MTOR SIGNALING.
    17. "The RSK factors of activating the Ras/MAPK signaling cascade."
      Carriere A., Ray H., Blenis J., Roux P.P.
      Front. Biosci. 13:4258-4275(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION, REVIEW ON ENZYME REGULATION.
    18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369; SER-375; SER-386; SER-415; SER-556 AND SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "The RSK family of kinases: emerging roles in cellular signalling."
      Anjum R., Blenis J.
      Nat. Rev. Mol. Cell Biol. 9:747-758(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION, REVIEW ON ENZYME REGULATION.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369 AND SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369; SER-375; SER-386; SER-415 AND SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. Cited for: VARIANTS CLS VAL-75 AND ALA-227.
    27. "Mutation analysis of the RSK2 gene in Coffin-Lowry patients: extensive allelic heterogeneity and a high rate of De novo mutations."
      Jacquot S., Merienne K., de Cesare D., Pannetier S., Mandel J.-L., Sassone-Corsi P., Hanauer A.
      Am. J. Hum. Genet. 63:1631-1640(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CLS PHE-82; GLN-127; TYR-154; VAL-225 AND ASP-431, VARIANT SER-38.
    28. "Novel mutations in Rsk-2, the gene for Coffin-Lowry syndrome (CLS)."
      Abidi F., Jacquot S., Lassiter C., Trivier E., Hanauer A., Schwartz C.E.
      Eur. J. Hum. Genet. 7:20-26(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CLS TRP-114 AND GLN-729.
    29. "Unreported RSK2 missense mutation in two male sibs with an unusually mild form of Coffin-Lowry syndrome."
      Manouvrier-Hanu S., Amiel J., Jacquot S., Merienne K., Moerman A., Coeslier A., Labarriere F., Vallee L., Croquette M.F., Hanauer A.
      J. Med. Genet. 36:775-778(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CLS LYS-189.
    30. "A missense mutation in RPS6KA3 (RSK2) responsible for non-specific mental retardation."
      Merienne K., Jacquot S., Pannetier S., Zeniou M., Bankier A., Gecz J., Mandel J.L., Mulley J., Sassone-Corsi P., Hanauer A.
      Nat. Genet. 22:13-14(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MRX19 TRP-383, CHARACTERIZATION OF VARIANT MRX19 TRP-383.
    31. "Intronic L1 insertion and F268S, novel mutations in RPS6KA3 (RSK2) causing Coffin-Lowry syndrome."
      Martinez-Garay I., Ballesta M.J., Oltra S., Orellana C., Palomeque A., Molto M.D., Prieto F., Martinez F.
      Clin. Genet. 64:491-496(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CLS SER-268.
    32. Cited for: VARIANT CLS ILE-477 DEL.
    33. "Mutations in the RSK2(RPS6KA3) gene cause Coffin-Lowry syndrome and nonsyndromic X-linked mental retardation."
      Field M., Tarpey P., Boyle J., Edkins S., Goodship J., Luo Y., Moon J., Teague J., Stratton M.R., Futreal P.A., Wooster R., Raymond F.L., Turner G.
      Clin. Genet. 70:509-515(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MRX19 SER-115; GLY-152 DEL AND ASP-202 DEL.
    34. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-416.
    35. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-38; CYS-483; PHE-608 AND CYS-723.

    Entry informationi

    Entry nameiKS6A3_HUMAN
    AccessioniPrimary (citable) accession number: P51812
    Secondary accession number(s): B2R9V4
    , Q4VAP3, Q59H26, Q5JPK8, Q7Z3Z7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 154 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3