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Q8C050

- KS6A5_MOUSE

UniProt

Q8C050 - KS6A5_MOUSE

Protein

Ribosomal protein S6 kinase alpha-5

Gene

Rps6ka5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (24 Oct 2003)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression. In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress. In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential. Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury.9 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by phosphorylation at Ser-359, Thr-645 and Thr-764 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha, and by further autophosphorylation of Ser-211, Ser-375 and Ser-380 by the activated C-terminal kinase domain. The active N-terminal kinase domain finally phosphorylates downstream substrates, as well as Ser-814, Ser-816 and Ser-822 in its own C-terminal region.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei80 – 801ATPPROSITE-ProRule annotation
    Active sitei176 – 1761Proton acceptorBy similarity
    Binding sitei454 – 4541ATPPROSITE-ProRule annotation
    Active sitei608 – 6081Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi54 – 629ATPPROSITE-ProRule annotation
    Nucleotide bindingi431 – 44010ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: InterPro
    3. protein binding Source: IntAct
    4. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. histone H2A-S1 phosphorylation Source: UniProtKB
    2. histone H3-S10 phosphorylation Source: UniProtKB
    3. histone H3-S28 phosphorylation Source: UniProtKB
    4. inflammatory response Source: UniProtKB-KW
    5. interleukin-1-mediated signaling pathway Source: Ensembl
    6. intracellular signal transduction Source: UniProtKB
    7. negative regulation of transcription, DNA-templated Source: UniProtKB
    8. positive regulation of histone acetylation Source: Ensembl
    9. positive regulation of histone phosphorylation Source: Ensembl
    10. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    11. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    12. protein phosphorylation Source: UniProtKB
    13. regulation of transcription, DNA-templated Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Inflammatory response, Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_215063. ERK/MAPK targets.
    REACT_224314. CREB phosphorylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal protein S6 kinase alpha-5 (EC:2.7.11.1)
    Short name:
    S6K-alpha-5
    Alternative name(s):
    90 kDa ribosomal protein S6 kinase 5
    Nuclear mitogen- and stress-activated protein kinase 1
    RSK-like protein kinase
    Short name:
    RLSK
    Gene namesi
    Name:Rps6ka5
    Synonyms:Msk1
    OrganismiMus musculus (Mouse)Imported
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1920336. Rps6ka5.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 863863Ribosomal protein S6 kinase alpha-5PRO_0000086208Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei211 – 2111Phosphoserine; by autocatalysisBy similarity
    Modified residuei359 – 3591Phosphoserine; by MAPK1, MAPK3 and MAPK14By similarity
    Modified residuei375 – 3751Phosphoserine; by autocatalysisBy similarity
    Modified residuei380 – 3801Phosphoserine; by autocatalysisBy similarity
    Modified residuei645 – 6451Phosphothreonine; by MAPK1, MAPK3 and MAPK14By similarity
    Modified residuei711 – 7111PhosphoserineBy similarity
    Modified residuei721 – 7211PhosphoserineBy similarity
    Modified residuei759 – 7591PhosphoserineBy similarity
    Modified residuei764 – 7641Phosphothreonine; by MAPK1, MAPK3 and MAPK14By similarity
    Modified residuei814 – 8141Phosphoserine; by autocatalysisBy similarity
    Modified residuei816 – 8161Phosphoserine; by autocatalysisBy similarity
    Modified residuei822 – 8221Phosphoserine; by autocatalysisBy similarity

    Post-translational modificationi

    Ser-375 and Thr-645 phosphorylation is required for kinase activity. Ser-375 and Ser-211 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-359, Thr-645 and Thr-764 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-814, Ser-816 and Ser-822 by the N-terminal kinase domain By similarity.By similarity
    Ubiquitinated.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8C050.
    PaxDbiQ8C050.
    PRIDEiQ8C050.

    PTM databases

    PhosphoSiteiQ8C050.

    Expressioni

    Gene expression databases

    BgeeiQ8C050.
    CleanExiMM_RPS6KA5.
    GenevestigatoriQ8C050.

    Interactioni

    Subunit structurei

    Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells which transiently dissociates following mitogenic stimulation. Also associates with MAPK14/p38-alpha. Activated RPS6KA5 associates with and phosphorylates the NF-kappa-B p65 subunit RELA. Interacts with CREBBP and EP300 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RaraP114162EBI-8391218,EBI-346736

    Protein-protein interaction databases

    BioGridi215759. 6 interactions.
    IntActiQ8C050. 2 interactions.
    MINTiMINT-4116279.
    STRINGi10090.ENSMUSP00000042987.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C050.
    SMRiQ8C050. Positions 23-379, 414-793.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini48 – 317270Protein kinase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini318 – 38669AGC-kinase C-terminalAdd
    BLAST
    Domaini428 – 675248Protein kinase 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110260.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiQ8C050.
    KOiK04445.
    OMAiFQSHDKS.
    OrthoDBiEOG76HQ0Z.
    PhylomeDBiQ8C050.
    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. 3 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. 3 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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2Curated (identifier: Q8C050-1) [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

    MEGEGGGSGG AGTSGDSGDG GEQLLTVKHE LRTANLTGHA EKVGIENFEL    50
    LKVLGTGAYG KVFLVRKISG HDAGKLYAMK VLKKATIVQK AKTTEHTRTE 100
    RQVLEHIRQS PFLVTLHYAF QTETKLHLIL DYINGGELFT HLSQRERFTE 150
    HEVQIYVGEI VLALEHLHKL GIIYRDIKLE NILLDSNGHV VLTDFGLSKE 200
    FVADETERAY SFCGTIEYMA PDIVRGGDSG HDKAVDWWSL GVLMYELLTG 250
    ASPFTVDGEK NSQAEISRRI LKSEPPYPQE MSTVAKDLLQ RLLMKDPKKR 300
    LGCGPRDAEE IKEHLFFEKI KWDDLAAKKV PAPFKPVIRD ELDVSNFAEE 350
    FTEMDPTYSP AALPQSSERL FQGYSFVAPS ILFKRNAAVI DPLQFHMGVD 400
    RPGVTNVARS AMMKDSPFYQ HYDLDLKDKP LGEGSFSICR KCVHKKTNQA 450
    FAVKIISKRM EANTQKEITA LKLCEGHPNI VKLHEVFHDQ VAASAQPPGQ 500
    VVLCSLLLLA LLFNRSLTRK PVTWTWLVHS TSQLPPLPPP MPEIVLFILL 550
    SDNGQLHTFL VMELLNGGEL FERIKRKKHF SETEASYIMR KLVSAVSHMH 600
    DVGVVHRDLK PENLLFTDEN DNLEIKVIDF GFARLKPPDN QPLKTPCFTL 650
    HYAAPELLTH NGYDESCDLW SLGVILYTML SGQVPFQSHD RSLTCTSAVE 700
    IMKKIKKGDF SFEGEAWKNV SQEAKDLIQG LLTVDPNKRL KMSGLRYNEW 750
    LQDGSQLSSN PLMTPDILGS SGAAVHTCVK ATFHAFNKYK REGFCLQNVD 800
    KAPLAKRRKM KRTSTSTETR SSSSESSRSS SSQSHGKTTP TKTLQPSNPT 850
    EGSNPDTLFQ FSD 863
    Length:863
    Mass (Da):96,583
    Last modified:October 24, 2003 - v2
    Checksum:i7A3C76D4036EA3EA
    GO
    Isoform 1Curated (identifier: Q8C050-2) [UniParc]FASTAAdd to Basket

    Also known as: 5Curated

    The sequence of this isoform differs from the canonical sequence as follows:
         490-554: Missing.

    Show »
    Length:798
    Mass (Da):89,515
    Checksum:i57AB12399BEF7B0E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 1514EGEGG…AGTSG → GGRAAAAAARAPAE in AAQ24165. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti117 – 1171H → N in BAC27809. (PubMed:16141072)Curated
    Sequence conflicti376 – 3761F → Y in BAC27809. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei490 – 55465Missing in isoform 1. 3 PublicationsVSP_050613Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY341873 mRNA. Translation: AAQ24158.1.
    AY341881 mRNA. Translation: AAQ24165.1.
    AK032316 mRNA. Translation: BAC27809.1.
    BC035298 mRNA. Translation: AAH35298.1.
    CCDSiCCDS26107.1. [Q8C050-1]
    RefSeqiNP_705815.1. NM_153587.2. [Q8C050-1]
    XP_006516337.1. XM_006516274.1. [Q8C050-2]
    UniGeneiMm.220417.
    Mm.392855.

    Genome annotation databases

    EnsembliENSMUST00000043599; ENSMUSP00000042987; ENSMUSG00000021180. [Q8C050-1]
    GeneIDi73086.
    KEGGimmu:73086.
    UCSCiuc007ost.1. mouse. [Q8C050-1]
    uc007osu.1. mouse. [Q8C050-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY341873 mRNA. Translation: AAQ24158.1 .
    AY341881 mRNA. Translation: AAQ24165.1 .
    AK032316 mRNA. Translation: BAC27809.1 .
    BC035298 mRNA. Translation: AAH35298.1 .
    CCDSi CCDS26107.1. [Q8C050-1 ]
    RefSeqi NP_705815.1. NM_153587.2. [Q8C050-1 ]
    XP_006516337.1. XM_006516274.1. [Q8C050-2 ]
    UniGenei Mm.220417.
    Mm.392855.

    3D structure databases

    ProteinModelPortali Q8C050.
    SMRi Q8C050. Positions 23-379, 414-793.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 215759. 6 interactions.
    IntActi Q8C050. 2 interactions.
    MINTi MINT-4116279.
    STRINGi 10090.ENSMUSP00000042987.

    PTM databases

    PhosphoSitei Q8C050.

    Proteomic databases

    MaxQBi Q8C050.
    PaxDbi Q8C050.
    PRIDEi Q8C050.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000043599 ; ENSMUSP00000042987 ; ENSMUSG00000021180 . [Q8C050-1 ]
    GeneIDi 73086.
    KEGGi mmu:73086.
    UCSCi uc007ost.1. mouse. [Q8C050-1 ]
    uc007osu.1. mouse. [Q8C050-2 ]

    Organism-specific databases

    CTDi 9252.
    MGIi MGI:1920336. Rps6ka5.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110260.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi Q8C050.
    KOi K04445.
    OMAi FQSHDKS.
    OrthoDBi EOG76HQ0Z.
    PhylomeDBi Q8C050.
    TreeFami TF313438.

    Enzyme and pathway databases

    Reactomei REACT_215063. ERK/MAPK targets.
    REACT_224314. CREB phosphorylation.

    Miscellaneous databases

    NextBioi 337443.
    PROi Q8C050.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8C050.
    CleanExi MM_RPS6KA5.
    Genevestigatori Q8C050.

    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. 3 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. 3 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 mouse ribosomal protein S6 kinase, 90kDa, polypeptide 5 (RPS6KA5)."
      Zhou G., Wang J., Xu W.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
    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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Brain.
    3. "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: Mammary gland.
    4. "Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1."
      Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M., Ma W.-Y., Dong Z.
      J. Biol. Chem. 276:33213-33219(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
    5. "MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse epidermal JB6 cells."
      Zhang Y., Liu G., Dong Z.
      J. Biol. Chem. 276:42534-42542(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF STAT3.
    6. "MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts."
      Wiggin G.R., Soloaga A., Foster J.M., Murray-Tait V., Cohen P., Arthur J.S.
      Mol. Cell. Biol. 22:2871-2881(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1 AND ATF1.
    7. "Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)."
      Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W., Haegeman G.
      EMBO J. 22:1313-1324(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Mitogen and stress response kinase-1 (MSK1) mediates excitotoxic induced death of hippocampal neurones."
      Hughes J.P., Staton P.C., Wilkinson M.G., Strijbos P.J., Skaper S.D., Arthur J.S., Reith A.D.
      J. Neurochem. 86:25-32(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL DEATH.
    9. "MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 or S28 via mitogen- and stress-activated kinase 1/2."
      Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J., Nightingale K., Iborra F.J., Mahadevan L.C.
      J. Cell Sci. 118:2247-2259(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
    10. "ERK1/2 and p38-MAPK signalling pathways, through MSK1, are involved in NF-kappaB transactivation during oxidative stress in skeletal myoblasts."
      Kefaloyianni E., Gaitanaki C., Beis I.
      Cell. Signal. 18:2238-2251(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RELA/NFKB3.
    11. "The kinases MSK1 and MSK2 are required for epidermal growth factor-induced, but not tumor necrosis factor-induced, histone H3 Ser10 phosphorylation."
      Duncan E.A., Anest V., Cogswell P., Baldwin A.S.
      J. Biol. Chem. 281:12521-12525(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
    12. "The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor signaling."
      Ananieva O., Darragh J., Johansen C., Carr J.M., McIlrath J., Park J.M., Wingate A., Monk C.E., Toth R., Santos S.G., Iversen L., Arthur J.S.
      Nat. Immunol. 9:1028-1036(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1; ATF1 AND HISTONE H3.

    Entry informationi

    Entry nameiKS6A5_MOUSE
    AccessioniPrimary (citable) accession number: Q8C050
    Secondary accession number(s): Q8CI92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2003
    Last sequence update: October 24, 2003
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Enzyme activity requires the presence of both kinase domains.By similarity

    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