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Q8BSK8

- KS6B1_MOUSE

UniProt

Q8BSK8 - KS6B1_MOUSE

Protein

Ribosomal protein S6 kinase beta-1

Gene

Rps6kb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression. Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex. Upon mitogenic stimulation, phosphorylation by the mammalian target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation. The active form then phosphorylates and activates several substrates in the preinitiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis. Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR. In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2. Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function. Phosphorylates mitochondrial RMP leading to dissociation of a RMP:PPP1CC complex. The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function. Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1. In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B. May be involved in cytoskeletal rearrangement through binding to neurabin. Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Activation requires multiple phosphorylation events on serine/threonine residues. Activation appears to be first mediated by phosphorylation of multiple sites in the autoinhibitory domain, which facilitates phosphorylation at Thr-412, disrupting the autoinhibitory mechanism and allowing phosphorylation of Thr-252 by PDPK1. The active conformation of the kinase is believed to be stabilized by a mechanism involving three conserved phosphorylation sites located in the kinase domain activation loop (Thr-252) and in the AGC-kinase C-terminal domain (Ser-394 in the middle of the tail/linker region and Thr-412 within a hydrophobic motif at its end). Activated by mTORC1; isoform Alpha I and isoform Alpha II are sensitive to rapamycin, which inhibits activating phosphorylation at Thr-412. Activated by PDPK1 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei123 – 1231ATPPROSITE-ProRule annotation
    Active sitei218 – 2181Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi97 – 1059ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. peptide binding Source: Ensembl
    3. protein binding Source: IntAct
    4. protein kinase activity Source: MGI
    5. protein serine/threonine/tyrosine kinase activity Source: MGI
    6. ribosomal protein S6 kinase activity Source: Ensembl

    GO - Biological processi

    1. aging Source: Ensembl
    2. apoptotic process Source: UniProtKB-KW
    3. cell migration Source: Ensembl
    4. cellular response to growth factor stimulus Source: UniProtKB
    5. cellular response to hormone stimulus Source: Ensembl
    6. G1/S transition of mitotic cell cycle Source: Ensembl
    7. germ cell development Source: MGI
    8. long-term memory Source: Ensembl
    9. negative regulation of apoptotic process Source: UniProtKB
    10. negative regulation of extrinsic apoptotic signaling pathway Source: MGI
    11. negative regulation of insulin receptor signaling pathway Source: Ensembl
    12. positive regulation of mitotic cell cycle Source: Ensembl
    13. positive regulation of skeletal muscle tissue growth Source: Ensembl
    14. positive regulation of smooth muscle cell migration Source: Ensembl
    15. positive regulation of smooth muscle cell proliferation Source: Ensembl
    16. positive regulation of translational initiation Source: Ensembl
    17. protein kinase B signaling Source: MGI
    18. protein phosphorylation Source: MGI
    19. regulation of glucose import Source: Ensembl
    20. response to drug Source: Ensembl
    21. response to electrical stimulus involved in regulation of muscle adaptation Source: Ensembl
    22. response to ethanol Source: Ensembl
    23. response to glucagon Source: Ensembl
    24. response to glucocorticoid Source: Ensembl
    25. response to glucose Source: Ensembl
    26. response to heat Source: Ensembl
    27. response to insulin Source: Ensembl
    28. response to leucine Source: Ensembl
    29. response to lipopolysaccharide Source: Ensembl
    30. response to mechanical stimulus Source: Ensembl
    31. response to nutrient Source: Ensembl
    32. response to testosterone Source: Ensembl
    33. response to toxic substance Source: Ensembl
    34. response to tumor necrosis factor Source: Ensembl
    35. response to wounding Source: Ensembl
    36. skeletal muscle atrophy Source: Ensembl
    37. skeletal muscle contraction Source: Ensembl
    38. TOR signaling Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle, Translation regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal protein S6 kinase beta-1 (EC:2.7.11.1)
    Short name:
    S6K-beta-1
    Short name:
    S6K1
    Alternative name(s):
    70 kDa ribosomal protein S6 kinase 1
    Short name:
    P70S6K1
    Short name:
    p70-S6K 1
    Ribosomal protein S6 kinase I
    Short name:
    S6K
    p70 ribosomal S6 kinase alpha
    Short name:
    p70 S6 kinase alpha
    Short name:
    p70 S6K-alpha
    Short name:
    p70 S6KA
    Gene namesi
    Name:Rps6kb1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1270849. Rps6kb1.

    Subcellular locationi

    Cytoplasm By similarity. Cell junctionsynapsesynaptosome By similarity. Mitochondrion outer membrane 1 Publication. Mitochondrion By similarity
    Note: Colocalizes with URI1 at mitochondrion.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell surface Source: Ensembl
    3. mitochondrial outer membrane Source: UniProtKB-SubCell
    4. mitochondrion Source: UniProtKB
    5. neuron projection Source: UniProtKB-SubCell
    6. nucleus Source: Ensembl
    7. perinuclear region of cytoplasm Source: Ensembl
    8. synapse Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Disruption phenotypei

    Impairment of body growth. Lethal in combination with Rps6kb2 deficiency.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 525525Ribosomal protein S6 kinase beta-1PRO_0000024344Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei252 – 2521Phosphothreonine; by PDPK1By similarity
    Modified residuei394 – 3941PhosphoserineBy similarity
    Modified residuei412 – 4121Phosphothreonine; by MTOR, NEK6 and NEK7By similarity
    Modified residuei434 – 4341PhosphoserineBy similarity
    Modified residuei441 – 4411PhosphoserineBy similarity
    Modified residuei444 – 4441PhosphothreonineBy similarity
    Modified residuei447 – 4471PhosphoserineBy similarity
    Modified residuei452 – 4521PhosphoserineBy similarity
    Modified residuei516 – 5161N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylation at Thr-412 is regulated by mTORC1. The phosphorylation at this site is maintained by an agonist-dependent autophosphorylation mechanism. Activated by phosphorylation at Thr-252 by PDPK1. Dephosphorylation by PPP1CC at Thr-412 in mitochondrion By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8BSK8.
    PaxDbiQ8BSK8.
    PRIDEiQ8BSK8.

    PTM databases

    PhosphoSiteiQ8BSK8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BSK8.
    BgeeiQ8BSK8.
    CleanExiMM_RPS6KB1.
    GenevestigatoriQ8BSK8.

    Interactioni

    Subunit structurei

    Interacts with PPP1R9A/neurabin-1 By similarity. Interacts with RPTOR. Interacts with IRS1. Interacts with EIF3B and EIF3C. Interacts with POLDIP3 and TRAF4 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Mdm2P238042EBI-646423,EBI-641788

    Protein-protein interaction databases

    BioGridi215408. 10 interactions.
    IntActiQ8BSK8. 5 interactions.
    MINTiMINT-5092082.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BSK8.
    SMRiQ8BSK8. Positions 81-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini91 – 352262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini353 – 42371AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni424 – 525102Autoinhibitory domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi28 – 325TOS motif

    Domaini

    The autoinhibitory domain is believed to block phosphorylation within the AGC-kinase C-terminal domain and the activation loop.By similarity
    The TOS (TOR signaling) motif is essential for activation by mTORC1.By similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000114960.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiQ5SWG1.
    KOiK04688.
    OMAiANRMPAR.
    OrthoDBiEOG7B8S38.
    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.
    IPR016238. Ribosomal_S6_kinase.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000605. Ribsml_S6_kin_1. 1 hit.
    SMARTiSM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform Alpha I (identifier: Q8BSK8-1) [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

    MRRRRRRDGF YLAPDFRHRE AEDMAGVFDI DLDQPEDAGS EDELEEGGQL    50
    NESMDHGGVG PYELGMEHCE KFEISETSVN RGPEKIRPEC FELLRVLGKG 100
    GYGKVFQVRK VTGANTGKIF AMKVLKKAMI VRNAKDTAHT KAERNILEEV 150
    KHPFIVDLIY AFQTGGKLYL ILEYLSGGEL FMQLEREGIF MEDTACFYLA 200
    EISMALGHLH QKGIIYRDLK PENIMLNHQG HVKLTDFGLC KESIHDGTVT 250
    HTFCGTIEYM APEILMRSGH NRAVDWWSLG ALMYDMLTGA PPFTGENRKK 300
    TIDKILKCKL NLPPYLTQEA RDLLKKLLKR NAASRLGAGP GDAGEVQAHP 350
    FFRHINWEEL LARKVEPPFK PLLQSEEDVS QFDSKFTRQT PVDSPDDSTL 400
    SESANQVFLG FTYVAPSVLE SVKEKFSFEP KIRSPRRFIG SPRTPVSPVK 450
    FSPGDFWGRG ASASTANPQT PVEYPMETSG IEQMDVTVSG EASAPLPIRQ 500
    PNSGPYKKQA FPMISKRPEH LRMNL 525
    Length:525
    Mass (Da):59,146
    Last modified:July 27, 2011 - v2
    Checksum:i5B3C09F6BB365EE2
    GO
    Isoform Alpha II (identifier: Q8BSK8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: Missing.

    Show »
    Length:502
    Mass (Da):56,157
    Checksum:i5AE6CF3FCAAE8B83
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601G → E in BAC28000. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323Missing in isoform Alpha II. CuratedVSP_018840Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK032724 mRNA. Translation: BAC28000.1.
    AL604063 Genomic DNA. Translation: CAI25799.1.
    CH466556 Genomic DNA. Translation: EDL15788.1.
    BC038491 mRNA. Translation: AAH38491.1.
    CCDSiCCDS48875.1. [Q8BSK8-1]
    RefSeqiNP_001107806.1. NM_001114334.1. [Q8BSK8-1]
    UniGeneiMm.394280.
    Mm.446624.
    Mm.479484.

    Genome annotation databases

    EnsembliENSMUST00000154617; ENSMUSP00000119715; ENSMUSG00000020516. [Q8BSK8-1]
    GeneIDi72508.
    KEGGimmu:72508.
    UCSCiuc007ksn.2. mouse. [Q8BSK8-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK032724 mRNA. Translation: BAC28000.1 .
    AL604063 Genomic DNA. Translation: CAI25799.1 .
    CH466556 Genomic DNA. Translation: EDL15788.1 .
    BC038491 mRNA. Translation: AAH38491.1 .
    CCDSi CCDS48875.1. [Q8BSK8-1 ]
    RefSeqi NP_001107806.1. NM_001114334.1. [Q8BSK8-1 ]
    UniGenei Mm.394280.
    Mm.446624.
    Mm.479484.

    3D structure databases

    ProteinModelPortali Q8BSK8.
    SMRi Q8BSK8. Positions 81-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 215408. 10 interactions.
    IntActi Q8BSK8. 5 interactions.
    MINTi MINT-5092082.

    Chemistry

    ChEMBLi CHEMBL5429.

    PTM databases

    PhosphoSitei Q8BSK8.

    Proteomic databases

    MaxQBi Q8BSK8.
    PaxDbi Q8BSK8.
    PRIDEi Q8BSK8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000154617 ; ENSMUSP00000119715 ; ENSMUSG00000020516 . [Q8BSK8-1 ]
    GeneIDi 72508.
    KEGGi mmu:72508.
    UCSCi uc007ksn.2. mouse. [Q8BSK8-1 ]

    Organism-specific databases

    CTDi 6198.
    MGIi MGI:1270849. Rps6kb1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000114960.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi Q5SWG1.
    KOi K04688.
    OMAi ANRMPAR.
    OrthoDBi EOG7B8S38.
    TreeFami TF313438.

    Miscellaneous databases

    NextBioi 336366.
    PROi Q8BSK8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BSK8.
    Bgeei Q8BSK8.
    CleanExi MM_RPS6KB1.
    Genevestigatori Q8BSK8.

    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.
    IPR016238. Ribosomal_S6_kinase.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000605. Ribsml_S6_kin_1. 1 hit.
    SMARTi SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Strain: Czech II.
      Tissue: Mammary tumor.
    5. "Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase."
      Wang X., Li W., Williams M., Terada N., Alessi D.R., Proud C.G.
      EMBO J. 20:4370-4379(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF EEF2K.
    6. "p70S6 kinase signals cell survival as well as growth, inactivating the pro-apoptotic molecule BAD."
      Harada H., Andersen J.S., Mann M., Terada N., Korsmeyer S.J.
      Proc. Natl. Acad. Sci. U.S.A. 98:9666-9670(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BAD, FUNCTION IN APOPTOSIS REGULATION, SUBCELLULAR LOCATION.
    7. "S6K1(-/-)/S6K2(-/-) mice exhibit perinatal lethality and rapamycin-sensitive 5'-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent S6 kinase pathway."
      Pende M., Um S.H., Mieulet V., Sticker M., Goss V.L., Mestan J., Mueller M., Fumagalli S., Kozma S.C., Thomas G.
      Mol. Cell. Biol. 24:3112-3124(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "S6K directly phosphorylates IRS-1 on Ser-270 to promote insulin resistance in response to TNF-(alpha) signaling through IKK2."
      Zhang J., Gao Z., Yin J., Quon M.J., Ye J.
      J. Biol. Chem. 283:35375-35382(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF IRS1.

    Entry informationi

    Entry nameiKS6B1_MOUSE
    AccessioniPrimary (citable) accession number: Q8BSK8
    Secondary accession number(s): Q5SWG1, Q8CHX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 116 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

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3