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Q9Z1M4

- KS6B2_MOUSE

UniProt

Q9Z1M4 - KS6B2_MOUSE

Protein

Ribosomal protein S6 kinase beta-2

Gene

Rps6kb2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Phosphorylates specifically ribosomal protein S6.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei99 – 991ATPPROSITE-ProRule annotation
    Active sitei194 – 1941Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi73 – 819ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. peptide binding Source: Ensembl
    3. protein kinase activity Source: MGI
    4. ribosomal protein S6 kinase activity Source: Ensembl

    GO - Biological processi

    1. positive regulation of translational initiation Source: Ensembl
    2. protein kinase B signaling Source: MGI
    3. protein phosphorylation Source: MGI

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 3474.
    ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_218211. AKT phosphorylates targets in the nucleus.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal protein S6 kinase beta-2 (EC:2.7.11.1)
    Short name:
    S6K-beta-2
    Short name:
    S6K2
    Alternative name(s):
    70 kDa ribosomal protein S6 kinase 2
    p70 ribosomal S6 kinase beta
    Short name:
    p70 S6 kinase beta
    Short name:
    p70 S6K-beta
    Short name:
    p70 S6KB
    Gene namesi
    Name:Rps6kb2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1927343. Rps6kb2.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 485485Ribosomal protein S6 kinase beta-2PRO_0000086215Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151PhosphoserineBy similarity
    Modified residuei420 – 4201Phosphothreonine1 Publication
    Modified residuei423 – 4231Phosphoserine1 Publication
    Modified residuei476 – 4761Phosphoserine; by PKCBy similarity

    Post-translational modificationi

    Phosphorylated and activated by MTOR. Phosphorylation by PKC within the NLS in response to mitogenic stimuli causes cytoplasmic retention.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9Z1M4.
    PRIDEiQ9Z1M4.

    PTM databases

    PhosphoSiteiQ9Z1M4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Z1M4.
    BgeeiQ9Z1M4.
    GenevestigatoriQ9Z1M4.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000025749.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z1M4.
    SMRiQ9Z1M4. Positions 58-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini67 – 328262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini329 – 39971AGC-kinase C-terminalAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi474 – 4807Nuclear localization signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi411 – 48575Pro-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000114960.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiQ9Z1M4.
    KOiK04688.
    OMAiHYEEIEI.
    OrthoDBiEOG7B8S38.
    PhylomeDBiQ9Z1M4.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9Z1M4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVFDLDLE TEEGSEGEGE PEFSPADVCP LGELRAAGLE TVGHYEEVEL    50
    TESSVNLGPE RIGPHCFELL SVLGKGGYGK VFQVRKVQGT NLGKIYAMKV 100
    LRKAKIVCSA KDTAHTRAER NILESVKHPF IVELAYAFQT GGKLYLILEC 150
    LSGGELFTHL EREGIFLEDT ACFYLAEITL ALGHLHSHGI IYRDLKPENI 200
    MLSSQGHIKL TDFGLCKESI HEGAITHTFC GTIEYMAPEI LVRTGHNRAV 250
    DWWSLGALMY DMLTGSPPFT AENRKKTMDK IIKGKLVLPP YLTPDARDLA 300
    KKFLKRNPTQ RIGGGLGDAA DVQRHPFFRH INWDDLLARR VDPPFRPSLQ 350
    SEEDVSQFDA RFTRQTPVDS PDDTALSESA NQAFLGFTYV APSVLDSIKE 400
    GFSFQPKLRS PRRLNSSPRT PISPLKFSPF EGFRPSPGPP EPMEPSLPPL 450
    LPSPPSPPPT STAPLPIRPP SGTKKSKKGR GRSGR 485
    Length:485
    Mass (Da):53,538
    Last modified:May 1, 1999 - v1
    Checksum:i396929ADAB0F6CB6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007938 mRNA. Translation: CAA07774.1.
    AK014412 mRNA. Translation: BAB29335.1.
    CCDSiCCDS29419.1.
    RefSeqiNP_067460.1. NM_021485.2.
    UniGeneiMm.271937.

    Genome annotation databases

    EnsembliENSMUST00000025749; ENSMUSP00000025749; ENSMUSG00000024830.
    ENSMUST00000181245; ENSMUSP00000137802; ENSMUSG00000097721.
    GeneIDi58988.
    KEGGimmu:58988.
    UCSCiuc008fzb.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007938 mRNA. Translation: CAA07774.1 .
    AK014412 mRNA. Translation: BAB29335.1 .
    CCDSi CCDS29419.1.
    RefSeqi NP_067460.1. NM_021485.2.
    UniGenei Mm.271937.

    3D structure databases

    ProteinModelPortali Q9Z1M4.
    SMRi Q9Z1M4. Positions 58-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000025749.

    PTM databases

    PhosphoSitei Q9Z1M4.

    Proteomic databases

    PaxDbi Q9Z1M4.
    PRIDEi Q9Z1M4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025749 ; ENSMUSP00000025749 ; ENSMUSG00000024830 .
    ENSMUST00000181245 ; ENSMUSP00000137802 ; ENSMUSG00000097721 .
    GeneIDi 58988.
    KEGGi mmu:58988.
    UCSCi uc008fzb.1. mouse.

    Organism-specific databases

    CTDi 6199.
    MGIi MGI:1927343. Rps6kb2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000114960.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi Q9Z1M4.
    KOi K04688.
    OMAi HYEEIEI.
    OrthoDBi EOG7B8S38.
    PhylomeDBi Q9Z1M4.
    TreeFami TF313438.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 3474.
    Reactomei REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_218211. AKT phosphorylates targets in the nucleus.

    Miscellaneous databases

    NextBioi 314486.
    PROi Q9Z1M4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z1M4.
    Bgeei Q9Z1M4.
    Genevestigatori Q9Z1M4.

    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. "Disruption of the p70(s6k)/p85(s6k) gene reveals a small mouse phenotype and a new functional S6 kinase."
      Shima H., Pende M., Chen Y., Fumagalli S., Thomas G., Kozma S.C.
      EMBO J. 17:6649-6659(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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.
      Tissue: Placenta.
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-420 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiKS6B2_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z1M4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 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