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Q15418

- KS6A1_HUMAN

UniProt

Q15418 - KS6A1_HUMAN

Protein

Ribosomal protein S6 kinase alpha-1

Gene

RPS6KA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (16 Apr 2002)
      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, 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.11 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-573 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-380, allowing binding of PDPK1, which in turn phosphorylates Ser-221 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei94 – 941ATPPROSITE-ProRule annotation
    Active sitei187 – 1871Proton acceptorBy similarity
    Binding sitei447 – 4471ATPPROSITE-ProRule annotation
    Active sitei535 – 5351Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi68 – 769ATPPROSITE-ProRule annotation
    Nucleotide bindingi424 – 4329ATPPROSITE-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 binding Source: IntAct
    5. protein serine/threonine/tyrosine kinase activity Source: MGI
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell cycle Source: UniProtKB-KW
    3. innate immune response Source: Reactome
    4. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    5. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    6. negative regulation of apoptotic process Source: UniProtKB
    7. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    8. neurotrophin TRK receptor signaling pathway Source: Reactome
    9. positive regulation of cell differentiation Source: UniProtKB
    10. positive regulation of cell growth Source: UniProtKB
    11. positive regulation of hepatic stellate cell activation 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. signal transduction Source: ProtInc
    16. stress-activated MAPK cascade Source: Reactome
    17. synaptic transmission Source: Reactome
    18. toll-like receptor 10 signaling pathway Source: Reactome
    19. toll-like receptor 2 signaling pathway Source: Reactome
    20. toll-like receptor 3 signaling pathway Source: Reactome
    21. toll-like receptor 4 signaling pathway Source: Reactome
    22. toll-like receptor 5 signaling pathway Source: Reactome
    23. toll-like receptor 9 signaling pathway Source: Reactome
    24. toll-like receptor signaling pathway Source: Reactome
    25. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    26. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    27. 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.
    SignaLinkiQ15418.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal protein S6 kinase alpha-1 (EC:2.7.11.1)
    Short name:
    S6K-alpha-1
    Alternative name(s):
    90 kDa ribosomal protein S6 kinase 1
    Short name:
    p90-RSK 1
    Short name:
    p90RSK1
    Short name:
    p90S6K
    MAP kinase-activated protein kinase 1a
    Short name:
    MAPK-activated protein kinase 1a
    Short name:
    MAPKAP kinase 1a
    Short name:
    MAPKAPK-1a
    Ribosomal S6 kinase 1
    Short name:
    RSK-1
    Gene namesi
    Name:RPS6KA1
    Synonyms:MAPKAPK1A, RSK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10430. RPS6KA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA
    5. spindle Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34845.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 735735Ribosomal protein S6 kinase alpha-1PRO_0000086198Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 541Phosphoserine1 Publication
    Modified residuei221 – 2211Phosphoserine; by PDPK11 Publication
    Modified residuei307 – 3071Phosphoserine1 Publication
    Modified residuei348 – 3481Phosphothreonine
    Modified residuei359 – 3591Phosphothreonine5 Publications
    Modified residuei363 – 3631Phosphoserine5 Publications
    Modified residuei369 – 3691Phosphoserine2 Publications
    Modified residuei380 – 3801Phosphoserine; by autocatalysis5 Publications
    Modified residuei573 – 5731Phosphothreonine1 Publication
    Modified residuei732 – 7321Phosphoserine1 Publication

    Post-translational modificationi

    Activated by phosphorylation at Ser-221 by PDPK1. Autophosphorylated on Ser-380, as part of the activation process. May be phosphorylated at Thr-359 and Ser-363 by MAPK1/ERK2 and MAPK3/ERK1.6 Publications
    N-terminal myristoylation results in an activated kinase in the absence of added growth factors.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15418.
    PaxDbiQ15418.
    PRIDEiQ15418.

    2D gel databases

    UCD-2DPAGEQ15418.

    PTM databases

    PhosphoSiteiQ15418.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15418.
    BgeeiQ15418.
    CleanExiHS_RPS6KA1.
    GenevestigatoriQ15418.

    Organism-specific databases

    HPAiCAB003852.
    HPA007981.

    Interactioni

    Subunit structurei

    Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation. Interacts with ETV1/ER81 and FGFR1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSP90AB1P082382EBI-963034,EBI-352572
    VASPP505524EBI-963034,EBI-748201

    Protein-protein interaction databases

    BioGridi112109. 57 interactions.
    DIPiDIP-29987N.
    IntActiQ15418. 28 interactions.
    MINTiMINT-207205.
    STRINGi9606.ENSP00000363277.

    Structurei

    Secondary structure

    1
    735
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi59 – 613
    Beta strandi62 – 7110
    Beta strandi74 – 818
    Beta strandi83 – 864
    Beta strandi90 – 967
    Beta strandi127 – 1337
    Beta strandi136 – 1416
    Helixi149 – 1568
    Helixi161 – 18020
    Helixi190 – 1923
    Beta strandi193 – 1953
    Beta strandi197 – 1993
    Beta strandi201 – 2033
    Helixi226 – 2283
    Helixi231 – 2344
    Helixi241 – 25717
    Helixi267 – 27610
    Helixi287 – 29610
    Turni301 – 3033
    Beta strandi307 – 3104
    Helixi312 – 3165
    Helixi319 – 3213
    Helixi326 – 3305
    Beta strandi418 – 42710
    Beta strandi430 – 4378
    Turni438 – 4403
    Beta strandi443 – 4508
    Helixi457 – 46610
    Beta strandi475 – 4806
    Beta strandi482 – 4898
    Helixi497 – 5026
    Beta strandi503 – 5053
    Helixi509 – 52820
    Helixi538 – 5403
    Beta strandi541 – 5455
    Helixi550 – 5523
    Beta strandi553 – 5553
    Turni574 – 5763
    Helixi588 – 60922
    Helixi622 – 63110
    Helixi639 – 6435
    Helixi646 – 65510
    Helixi660 – 6623
    Helixi666 – 6705
    Helixi673 – 6764
    Helixi678 – 6803
    Helixi691 – 70717
    Helixi717 – 7193
    Helixi721 – 7244

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WNTX-ray2.40A/B413-719[»]
    2Z7QX-ray2.00A33-353[»]
    2Z7RX-ray2.00A33-353[»]
    2Z7SX-ray2.10A33-353[»]
    3RNYX-ray2.70A/B411-735[»]
    3TEIX-ray2.40B712-735[»]
    4H3PX-ray2.30B/E712-735[»]
    ProteinModelPortaliQ15418.
    SMRiQ15418. Positions 10-709.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15418.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini62 – 321260Protein kinase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini322 – 39170AGC-kinase C-terminalAdd
    BLAST
    Domaini418 – 675258Protein 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.
    HOVERGENiHBG108317.
    KOiK04373.
    OMAiPWITQKD.
    OrthoDBiEOG7B8S38.
    PhylomeDBiQ15418.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15418-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPLAQLKEPW PLMELVPLDP ENGQTSGEEA GLQPSKDEGV LKEISITHHV    50
    KAGSEKADPS HFELLKVLGQ GSFGKVFLVR KVTRPDSGHL YAMKVLKKAT 100
    LKVRDRVRTK MERDILADVN HPFVVKLHYA FQTEGKLYLI LDFLRGGDLF 150
    TRLSKEVMFT EEDVKFYLAE LALGLDHLHS LGIIYRDLKP ENILLDEEGH 200
    IKLTDFGLSK EAIDHEKKAY SFCGTVEYMA PEVVNRQGHS HSADWWSYGV 250
    LMFEMLTGSL PFQGKDRKET MTLILKAKLG MPQFLSTEAQ SLLRALFKRN 300
    PANRLGSGPD GAEEIKRHVF YSTIDWNKLY RREIKPPFKP AVAQPDDTFY 350
    FDTEFTSRTP KDSPGIPPSA GAHQLFRGFS FVATGLMEDD GKPRAPQAPL 400
    HSVVQQLHGK NLVFSDGYVV KETIGVGSYS ECKRCVHKAT NMEYAVKVID 450
    KSKRDPSEEI EILLRYGQHP NIITLKDVYD DGKHVYLVTE LMRGGELLDK 500
    ILRQKFFSER EASFVLHTIG KTVEYLHSQG VVHRDLKPSN ILYVDESGNP 550
    ECLRICDFGF AKQLRAENGL LMTPCYTANF VAPEVLKRQG YDEGCDIWSL 600
    GILLYTMLAG YTPFANGPSD TPEEILTRIG SGKFTLSGGN WNTVSETAKD 650
    LVSKMLHVDP HQRLTAKQVL QHPWVTQKDK LPQSQLSHQD LQLVKGAMAA 700
    TYSALNSSKP TPQLKPIESS ILAQRRVRKL PSTTL 735
    Length:735
    Mass (Da):82,723
    Last modified:April 16, 2002 - v2
    Checksum:i765731A4442A53DF
    GO
    Isoform 2 (identifier: Q15418-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: MPLAQLKEPW...GEEAGLQPSK → MEQDPKPPRL...GPGSGPQRDS

    Show »
    Length:744
    Mass (Da):83,932
    Checksum:i3121E64369EBDBBF
    GO
    Isoform 3 (identifier: Q15418-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-92: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:643
    Mass (Da):72,698
    Checksum:iB8362021FCCC17B5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti609 – 6091A → T in BAF85411. (PubMed:14702039)Curated
    Sequence conflicti619 – 6191S → G in BAF85411. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti335 – 3351K → T.2 Publications
    Corresponds to variant rs2229712 [ dbSNP | Ensembl ].
    VAR_021864

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9292Missing in isoform 3. 1 PublicationVSP_041580Add
    BLAST
    Alternative sequencei1 – 3636MPLAQ…LQPSK → MEQDPKPPRLRLWALIPWLP RKQRPRISQTSLPVPGPGSG PQRDS in isoform 2. 1 PublicationVSP_041380Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07597 mRNA. Translation: AAC82497.1.
    AK292722 mRNA. Translation: BAF85411.1.
    AK299007 mRNA. Translation: BAH12926.1.
    AK315730 mRNA. Translation: BAG38085.1.
    AL109743 Genomic DNA. Translation: CAC36348.1.
    AL627313 Genomic DNA. Translation: CAI14647.1.
    AL627313 Genomic DNA. Translation: CAI14648.1.
    AL627313 Genomic DNA. Translation: CAI14649.1.
    CH471059 Genomic DNA. Translation: EAX07799.1.
    BC014966 mRNA. Translation: AAH14966.1.
    CCDSiCCDS284.1. [Q15418-1]
    CCDS30649.1. [Q15418-2]
    PIRiI51901.
    RefSeqiNP_001006666.1. NM_001006665.1. [Q15418-2]
    NP_002944.2. NM_002953.3. [Q15418-1]
    XP_005246024.1. XM_005245967.2. [Q15418-3]
    UniGeneiHs.149957.

    Genome annotation databases

    EnsembliENST00000374168; ENSP00000363283; ENSG00000117676. [Q15418-1]
    ENST00000526792; ENSP00000431651; ENSG00000117676. [Q15418-3]
    ENST00000531382; ENSP00000435412; ENSG00000117676. [Q15418-2]
    GeneIDi6195.
    KEGGihsa:6195.
    UCSCiuc001bmr.1. human. [Q15418-1]
    uc001bms.1. human. [Q15418-2]

    Polymorphism databases

    DMDMi20178306.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07597 mRNA. Translation: AAC82497.1 .
    AK292722 mRNA. Translation: BAF85411.1 .
    AK299007 mRNA. Translation: BAH12926.1 .
    AK315730 mRNA. Translation: BAG38085.1 .
    AL109743 Genomic DNA. Translation: CAC36348.1 .
    AL627313 Genomic DNA. Translation: CAI14647.1 .
    AL627313 Genomic DNA. Translation: CAI14648.1 .
    AL627313 Genomic DNA. Translation: CAI14649.1 .
    CH471059 Genomic DNA. Translation: EAX07799.1 .
    BC014966 mRNA. Translation: AAH14966.1 .
    CCDSi CCDS284.1. [Q15418-1 ]
    CCDS30649.1. [Q15418-2 ]
    PIRi I51901.
    RefSeqi NP_001006666.1. NM_001006665.1. [Q15418-2 ]
    NP_002944.2. NM_002953.3. [Q15418-1 ]
    XP_005246024.1. XM_005245967.2. [Q15418-3 ]
    UniGenei Hs.149957.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WNT X-ray 2.40 A/B 413-719 [» ]
    2Z7Q X-ray 2.00 A 33-353 [» ]
    2Z7R X-ray 2.00 A 33-353 [» ]
    2Z7S X-ray 2.10 A 33-353 [» ]
    3RNY X-ray 2.70 A/B 411-735 [» ]
    3TEI X-ray 2.40 B 712-735 [» ]
    4H3P X-ray 2.30 B/E 712-735 [» ]
    ProteinModelPortali Q15418.
    SMRi Q15418. Positions 10-709.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112109. 57 interactions.
    DIPi DIP-29987N.
    IntActi Q15418. 28 interactions.
    MINTi MINT-207205.
    STRINGi 9606.ENSP00000363277.

    Chemistry

    BindingDBi Q15418.
    ChEMBLi CHEMBL2553.
    GuidetoPHARMACOLOGYi 1527.

    PTM databases

    PhosphoSitei Q15418.

    Polymorphism databases

    DMDMi 20178306.

    2D gel databases

    UCD-2DPAGE Q15418.

    Proteomic databases

    MaxQBi Q15418.
    PaxDbi Q15418.
    PRIDEi Q15418.

    Protocols and materials databases

    DNASUi 6195.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374168 ; ENSP00000363283 ; ENSG00000117676 . [Q15418-1 ]
    ENST00000526792 ; ENSP00000431651 ; ENSG00000117676 . [Q15418-3 ]
    ENST00000531382 ; ENSP00000435412 ; ENSG00000117676 . [Q15418-2 ]
    GeneIDi 6195.
    KEGGi hsa:6195.
    UCSCi uc001bmr.1. human. [Q15418-1 ]
    uc001bms.1. human. [Q15418-2 ]

    Organism-specific databases

    CTDi 6195.
    GeneCardsi GC01P026856.
    HGNCi HGNC:10430. RPS6KA1.
    HPAi CAB003852.
    HPA007981.
    MIMi 601684. gene.
    neXtProti NX_Q15418.
    PharmGKBi PA34845.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108317.
    KOi K04373.
    OMAi PWITQKD.
    OrthoDBi EOG7B8S38.
    PhylomeDBi Q15418.
    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 Q15418.

    Miscellaneous databases

    ChiTaRSi RPS6KA1. human.
    EvolutionaryTracei Q15418.
    GeneWikii RPS6KA1.
    GenomeRNAii 6195.
    NextBioi 24057.
    PROi Q15418.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15418.
    Bgeei Q15418.
    CleanExi HS_RPS6KA1.
    Genevestigatori Q15418.

    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 ]
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    Publicationsi

    1. "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] (ISOFORM 1), VARIANT THR-335.
    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] (ISOFORMS 1; 2 AND 3).
      Tissue: Testis and Thyroid.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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] (ISOFORM 1).
      Tissue: Colon.
    6. "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB."
      Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.
      EMBO J. 17:4426-4441(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK."
      Dalby K.N., Morrice N., Caudwell F.B., Avruch J., Cohen P.
      J. Biol. Chem. 273:1496-1505(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732.
    8. "Rsk1 mediates a MEK-MAP kinase cell survival signal."
      Shimamura A., Ballif B.A., Richards S.A., Blenis J.
      Curr. Biol. 10:127-135(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BAD.
    9. "C/EBPbeta phosphorylation by RSK creates a functional XEXD caspase inhibitory box critical for cell survival."
      Buck M., Poli V., Hunter T., Chojkier M.
      Mol. Cell 8:807-816(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CEBPB.
    10. "Regulation of the ETS transcription factor ER81 by the 90-kDa ribosomal S6 kinase 1 and protein kinase A."
      Wu J., Janknecht R.
      J. Biol. Chem. 277:42669-42679(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF ETV1/ER81, INTERACTION WITH ETV1/ER81.
    11. "Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity."
      Roux P.P., Richards S.A., Blenis J.
      Mol. Cell. Biol. 23:4796-4804(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK1 OR MAPK3.
    12. "90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling."
      Hu Y., Fang X., Dunham S.M., Prada C., Stachowiak E.K., Stachowiak M.K.
      J. Biol. Chem. 279:29325-29335(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FGFR1, ENZYME REGULATION, SUBCELLULAR LOCATION.
    13. "Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase."
      Roux P.P., Ballif B.A., Anjum R., Gygi S.P., Blenis J.
      Proc. Natl. Acad. Sci. U.S.A. 101:13489-13494(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MTOR SIGNALING, INTERACTION WITH TSC2.
    14. "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.
    15. "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.
    16. "The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity."
      Shahbazian D., Roux P.P., Mieulet V., Cohen M.S., Raught B., Taunton J., Hershey J.W., Blenis J., Pende M., Sonenberg N.
      EMBO J. 25:2781-2791(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSLATION REGULATION, FUNCTION IN PHOSPHORYLATION OF EIF4B.
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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.
    19. "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.
    20. "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.
    21. "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-359; SER-363 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "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.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-307; THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "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-359 AND SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Crystal structures of the N-terminal kinase domain of human RSK1 bound to three different ligands: Implications for the design of RSK1 specific inhibitors."
      Ikuta M., Kornienko M., Byrne N., Reid J.C., Mizuarai S., Kotani H., Munshi S.K.
      Protein Sci. 16:2626-2635(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 33-353 IN COMPLEX WITH INHIBITOR.
    29. "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: VARIANT [LARGE SCALE ANALYSIS] THR-335.

    Entry informationi

    Entry nameiKS6A1_HUMAN
    AccessioniPrimary (citable) accession number: Q15418
    Secondary accession number(s): A6NGG4
    , A8K9K7, B2RDY8, B7Z5J0, Q5SVM5, Q5SVM8, Q5SVM9, Q96C05, Q9BQK2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 157 of the entry and version 2 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 1
      Human chromosome 1: 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