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O75676

- KS6A4_HUMAN

UniProt

O75676 - KS6A4_HUMAN

Protein

Ribosomal protein S6 kinase alpha-4

Gene

RPS6KA4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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 factor RELA, 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. 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.3 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    Activated by phosphorylation at Ser-343, Thr-568 and Thr-687 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha, and by further autophosphorylation of Ser-196, Ser-360 and Ser-365 by the activated C-terminal kinase domain.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei65 – 651ATPPROSITE-ProRule annotation
    Active sitei161 – 1611Proton acceptorBy similarity
    Binding sitei440 – 4401ATPPROSITE-ProRule annotation
    Active sitei530 – 5301Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi39 – 479ATPPROSITE-ProRule annotation
    Nucleotide bindingi417 – 4259ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: InterPro
    3. mitogen-activated protein kinase p38 binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein serine/threonine kinase activity Source: UniProtKB
    6. ribosomal protein S6 kinase activity Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. histone H3-S10 phosphorylation Source: UniProtKB
    3. histone H3-S28 phosphorylation Source: UniProtKB
    4. histone phosphorylation Source: BHF-UCL
    5. inflammatory response Source: UniProtKB-KW
    6. interleukin-1-mediated signaling pathway Source: BHF-UCL
    7. intracellular signal transduction Source: UniProtKB
    8. negative regulation of cytokine production Source: UniProtKB
    9. positive regulation of CREB transcription factor activity Source: UniProtKB
    10. positive regulation of histone acetylation Source: BHF-UCL
    11. positive regulation of histone phosphorylation Source: BHF-UCL
    12. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    13. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    14. protein phosphorylation Source: UniProtKB
    15. 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, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_22365. Recycling pathway of L1.
    SignaLinkiO75676.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal protein S6 kinase alpha-4 (EC:2.7.11.1)
    Short name:
    S6K-alpha-4
    Alternative name(s):
    90 kDa ribosomal protein S6 kinase 4
    Nuclear mitogen- and stress-activated protein kinase 2
    Ribosomal protein kinase B
    Short name:
    RSKB
    Gene namesi
    Name:RPS6KA4
    Synonyms:MSK2
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:10433. RPS6KA4.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi709 – 7091F → A: Strongly elevates basal activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA34848.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 772772Ribosomal protein S6 kinase alpha-4PRO_0000086205Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei196 – 1961Phosphoserine; by autocatalysisBy similarity
    Modified residuei343 – 3431Phosphoserine; by MAPK1, MAPK3 and MAPK14Curated
    Modified residuei347 – 3471Phosphoserine2 Publications
    Modified residuei360 – 3601Phosphoserine; by autocatalysisBy similarity
    Modified residuei365 – 3651Phosphoserine; by autocatalysisBy similarity
    Modified residuei542 – 5421Phosphothreonine1 Publication
    Modified residuei568 – 5681Phosphothreonine; by MAPK1, MAPK3 and MAPK14By similarity
    Modified residuei634 – 6341Phosphoserine1 Publication
    Modified residuei678 – 6781Phosphoserine1 Publication
    Modified residuei687 – 6871Phosphothreonine2 Publications
    Modified residuei737 – 7371Phosphoserine; by autocatalysisCurated
    Modified residuei745 – 7451Phosphoserine1 Publication

    Post-translational modificationi

    Ser-343 and Thr-568 phosphorylation is required for kinase activity. Ser-343 and Ser-196 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-343, Thr-568 and Thr-687 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-737 and Ser-745 by the N-terminal kinase domain By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75676.
    PaxDbiO75676.
    PRIDEiO75676.

    PTM databases

    PhosphoSiteiO75676.

    Expressioni

    Gene expression databases

    ArrayExpressiO75676.
    BgeeiO75676.
    CleanExiHS_RPS6KA4.
    GenevestigatoriO75676.

    Organism-specific databases

    HPAiCAB008649.
    HPA023225.

    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 RPS6KA4 associates with and phosphorylates the NF-kappa-B p65 subunit RELA.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAPK14Q165393EBI-73933,EBI-73946

    Protein-protein interaction databases

    BioGridi114468. 13 interactions.
    IntActiO75676. 5 interactions.
    MINTiMINT-7944429.
    STRINGi9606.ENSP00000333896.

    Structurei

    3D structure databases

    ProteinModelPortaliO75676.
    SMRiO75676. Positions 13-365, 369-716.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 301269Protein kinase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini302 – 37170AGC-kinase C-terminalAdd
    BLAST
    Domaini411 – 674264Protein kinase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni725 – 77248Required for nuclear targeting and association with MAPK14Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiO75676.
    KOiK16510.
    OMAiYHTYLVM.
    PhylomeDBiO75676.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75676-1) [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

    MGDEDDDESC AVELRITEAN LTGHEEKVSV ENFELLKVLG TGAYGKVFLV    50
    RKAGGHDAGK LYAMKVLRKA ALVQRAKTQE HTRTERSVLE LVRQAPFLVT 100
    LHYAFQTDAK LHLILDYVSG GEMFTHLYQR QYFKEAEVRV YGGEIVLALE 150
    HLHKLGIIYR DLKLENVLLD SEGHIVLTDF GLSKEFLTEE KERTFSFCGT 200
    IEYMAPEIIR SKTGHGKAVD WWSLGILLFE LLTGASPFTL EGERNTQAEV 250
    SRRILKCSPP FPPRIGPVAQ DLLQRLLCKD PKKRLGAGPQ GAQEVRNHPF 300
    FQGLDWVALA ARKIPAPFRP QIRSELDVGN FAEEFTRLEP VYSPPGSPPP 350
    GDPRIFQGYS FVAPSILFDH NNAVMTDGLE APGAGDRPGR AAVARSAMMQ 400
    DSPFFQQYEL DLREPALGQG SFSVCRRCRQ RQSGQEFAVK ILSRRLEANT 450
    QREVAALRLC QSHPNVVNLH EVHHDQLHTY LVLELLRGGE LLEHIRKKRH 500
    FSESEASQIL RSLVSAVSFM HEEAGVVHRD LKPENILYAD DTPGAPVKII 550
    DFGFARLRPQ SPGVPMQTPC FTLQYAAPEL LAQQGYDESC DLWSLGVILY 600
    MMLSGQVPFQ GASGQGGQSQ AAEIMCKIRE GRFSLDGEAW QGVSEEAKEL 650
    VRGLLTVDPA KRLKLEGLRG SSWLQDGSAR SSPPLRTPDV LESSGPAVRS 700
    GLNATFMAFN RGKREGFFLK SVENAPLAKR RKQKLRSATA SRRGSPAPAN 750
    PGRAPVASKG APRRANGPLP PS 772
    Length:772
    Mass (Da):85,606
    Last modified:November 1, 1998 - v1
    Checksum:i3606209693D0B5F3
    GO
    Isoform 2 (identifier: O75676-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         401-406: Missing.

    Show »
    Length:766
    Mass (Da):84,884
    Checksum:iDE27817E248DA71E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti477 – 4771L → P in BAD97281. 1 PublicationCurated
    Isoform 2 (identifier: O75676-2)
    Sequence conflicti400 – 4012QQ → Q in BAD97281. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti236 – 2361S → L in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
    VAR_040632
    Natural varianti758 – 7581S → A.2 Publications
    Corresponds to variant rs17857342 [ dbSNP | Ensembl ].
    VAR_040633

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei401 – 4066Missing in isoform 2. 2 PublicationsVSP_017733

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ010119 mRNA. Translation: CAA09009.1.
    AK223561 mRNA. Translation: BAD97281.1.
    AK292163 mRNA. Translation: BAF84852.1.
    CH471076 Genomic DNA. Translation: EAW74260.1.
    AF074715 mRNA. Translation: AAC67395.1.
    CCDSiCCDS8073.1. [O75676-1]
    RefSeqiNP_001006945.1. NM_001006944.1. [O75676-2]
    NP_003933.1. NM_003942.2. [O75676-1]
    UniGeneiHs.105584.

    Genome annotation databases

    EnsembliENST00000334205; ENSP00000333896; ENSG00000162302. [O75676-1]
    GeneIDi8986.
    KEGGihsa:8986.
    UCSCiuc001oad.3. human. [O75676-2]
    uc001oae.3. human. [O75676-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ010119 mRNA. Translation: CAA09009.1 .
    AK223561 mRNA. Translation: BAD97281.1 .
    AK292163 mRNA. Translation: BAF84852.1 .
    CH471076 Genomic DNA. Translation: EAW74260.1 .
    AF074715 mRNA. Translation: AAC67395.1 .
    CCDSi CCDS8073.1. [O75676-1 ]
    RefSeqi NP_001006945.1. NM_001006944.1. [O75676-2 ]
    NP_003933.1. NM_003942.2. [O75676-1 ]
    UniGenei Hs.105584.

    3D structure databases

    ProteinModelPortali O75676.
    SMRi O75676. Positions 13-365, 369-716.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114468. 13 interactions.
    IntActi O75676. 5 interactions.
    MINTi MINT-7944429.
    STRINGi 9606.ENSP00000333896.

    Chemistry

    BindingDBi O75676.
    ChEMBLi CHEMBL3125.
    GuidetoPHARMACOLOGYi 1524.

    PTM databases

    PhosphoSitei O75676.

    Proteomic databases

    MaxQBi O75676.
    PaxDbi O75676.
    PRIDEi O75676.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334205 ; ENSP00000333896 ; ENSG00000162302 . [O75676-1 ]
    GeneIDi 8986.
    KEGGi hsa:8986.
    UCSCi uc001oad.3. human. [O75676-2 ]
    uc001oae.3. human. [O75676-1 ]

    Organism-specific databases

    CTDi 8986.
    GeneCardsi GC11P064126.
    HGNCi HGNC:10433. RPS6KA4.
    HPAi CAB008649.
    HPA023225.
    MIMi 603606. gene.
    neXtProti NX_O75676.
    PharmGKBi PA34848.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi O75676.
    KOi K16510.
    OMAi YHTYLVM.
    PhylomeDBi O75676.
    TreeFami TF313438.

    Enzyme and pathway databases

    Reactomei REACT_22365. Recycling pathway of L1.
    SignaLinki O75676.

    Miscellaneous databases

    GeneWikii RPS6KA4.
    GenomeRNAii 8986.
    NextBioi 33697.
    PROi O75676.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75676.
    Bgeei O75676.
    CleanExi HS_RPS6KA4.
    Genevestigatori O75676.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR016239. Ribosomal_S6_kinase_II.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 2 hits.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000606. Ribsml_S6_kin_2. 1 hit.
    SMARTi SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 2 hits.
    PS50011. PROTEIN_KINASE_DOM. 2 hits.
    PS00108. PROTEIN_KINASE_ST. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase under dominant control of p38alpha mitogen-activated protein kinase (p38alphaMAPK)."
      Pierrat B., Correia J.D.S., Mary J.L., Tomas-Zuber M., Lesslauer W.
      J. Biol. Chem. 273:29661-29671(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, INTERACTION WITH MAPK14; MAPK1 AND MAPK3, SUBCELLULAR LOCATION.
      Tissue: PlacentaImported.
    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] (ISOFORM 1).
      Tissue: Synovium.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ALA-758.
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 17-727 (ISOFORM 2).
    6. "C-terminal elements control location, activation threshold, and p38 docking of ribosomal S6 kinase B (RSKB)."
      Tomas-Zuber M., Mary J.L., Lamour F., Bur D., Lesslauer W.
      J. Biol. Chem. 276:5892-5899(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAPK14, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-709.
    7. "MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14."
      Soloaga A., Thomson S., Wiggin G.R., Rampersaud N., Dyson M.H., Hazzalin C.A., Mahadevan L.C., Arthur J.S.
      EMBO J. 22:2788-2797(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3 AND HMGN1/HMG14.
    8. "MSK activation and physiological roles."
      Arthur J.S.
      Front. Biosci. 13:5866-5879(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    9. "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 SER-347; SER-634; SER-678; THR-687 AND SER-745, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; THR-542 AND THR-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: REVIEW ON FUNCTION.
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-236 AND ALA-758.

    Entry informationi

    Entry nameiKS6A4_HUMAN
    AccessioniPrimary (citable) accession number: O75676
    Secondary accession number(s): A8K7Z8, O75585, Q53ES8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2003
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3