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Q15349

- KS6A2_HUMAN

UniProt

Q15349 - KS6A2_HUMAN

Protein

Ribosomal protein S6 kinase alpha-2

Gene

RPS6KA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (21 Mar 2006)
      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 transcription factors, regulates translation, and mediates cellular proliferation, survival, and differentiation. May function as tumor suppressor in epithelial ovarian cancer cells.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-570 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-377, allowing binding of PDPK1, which in turn phosphorylates Ser-218 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei91 – 911ATPPROSITE-ProRule annotation
    Active sitei184 – 1841Proton acceptorBy similarity
    Binding sitei444 – 4441ATPPROSITE-ProRule annotation
    Active sitei532 – 5321Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi65 – 739ATPPROSITE-ProRule annotation
    Nucleotide bindingi421 – 4299ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. brain renin-angiotensin system Source: Ensembl
    3. cardiac muscle cell apoptotic process Source: Ensembl
    4. cellular response to carbohydrate stimulus Source: Ensembl
    5. heart contraction Source: Ensembl
    6. heart development Source: Ensembl
    7. innate immune response Source: Reactome
    8. intracellular signal transduction Source: ProtInc
    9. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    10. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    11. negative regulation of cell cycle Source: UniProtKB
    12. negative regulation of cell proliferation Source: UniProtKB
    13. negative regulation of meiosis Source: Ensembl
    14. neurotrophin TRK receptor signaling pathway Source: Reactome
    15. oocyte maturation Source: Ensembl
    16. peptidyl-serine phosphorylation Source: Ensembl
    17. positive regulation of apoptotic process Source: UniProtKB
    18. positive regulation of gene expression Source: Ensembl
    19. regulation of protein processing Source: Ensembl
    20. signal transduction Source: ProtInc
    21. stress-activated MAPK cascade Source: Reactome
    22. synaptic transmission Source: Reactome
    23. toll-like receptor 10 signaling pathway Source: Reactome
    24. toll-like receptor 2 signaling pathway Source: Reactome
    25. toll-like receptor 3 signaling pathway Source: Reactome
    26. toll-like receptor 4 signaling pathway Source: Reactome
    27. toll-like receptor 5 signaling pathway Source: Reactome
    28. toll-like receptor 9 signaling pathway Source: Reactome
    29. toll-like receptor signaling pathway Source: Reactome
    30. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    31. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    32. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    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.
    SignaLinkiQ15349.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal protein S6 kinase alpha-2 (EC:2.7.11.1)
    Short name:
    S6K-alpha-2
    Alternative name(s):
    90 kDa ribosomal protein S6 kinase 2
    Short name:
    p90-RSK 2
    Short name:
    p90RSK2
    MAP kinase-activated protein kinase 1c
    Short name:
    MAPK-activated protein kinase 1c
    Short name:
    MAPKAP kinase 1c
    Short name:
    MAPKAPK-1c
    Ribosomal S6 kinase 3
    Short name:
    RSK-3
    pp90RSK3
    Gene namesi
    Name:RPS6KA2
    Synonyms:MAPKAPK1C, RSK3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10431. RPS6KA2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA34846.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 733733Ribosomal protein S6 kinase alpha-2PRO_0000086201Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei218 – 2181Phosphoserine; by PDPK11 Publication
    Modified residuei377 – 3771Phosphoserine1 Publication
    Cross-linki630 – 630Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Activated by phosphorylation at Ser-218 by PDPK1. Autophosphorylated on Ser-377, as part of the activation process. May be phosphorylated at Thr-356 and Ser-360 by MAPK1/ERK2 and MAPK3/ERK1 By similarity.By similarity
    N-terminal myristoylation results in an activated kinase in the absence of added growth factors.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15349.
    PaxDbiQ15349.
    PRIDEiQ15349.

    2D gel databases

    REPRODUCTION-2DPAGEQ15349.

    PTM databases

    PhosphoSiteiQ15349.

    Expressioni

    Tissue specificityi

    Widely expressed with higher expression in lung, skeletal muscle, brain, uterus, ovary, thyroid and prostate.2 Publications

    Gene expression databases

    ArrayExpressiQ15349.
    BgeeiQ15349.
    CleanExiHS_RPS6KA2.
    GenevestigatoriQ15349.

    Organism-specific databases

    HPAiCAB026243.
    HPA045061.
    HPA054237.

    Interactioni

    Subunit structurei

    Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRAFP150562EBI-1384149,EBI-365980
    MAPK3P273612EBI-1384149,EBI-73995
    PRKCEQ021562EBI-1384149,EBI-706254

    Protein-protein interaction databases

    BioGridi112110. 13 interactions.
    DIPiDIP-295N.
    IntActiQ15349. 11 interactions.
    MINTiMINT-1542928.
    STRINGi9606.ENSP00000386050.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15349.
    SMRiQ15349. Positions 24-704.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini59 – 318260Protein kinase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini319 – 38870AGC-kinase C-terminalAdd
    BLAST
    Domaini415 – 672258Protein 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.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    KOiK04373.
    OrthoDBiEOG7B8S38.
    PhylomeDBiQ15349.
    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: Q15349-1) [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

    MDLSMKKFAV RRFFSVYLRR KSRSKSSSLS RLEEEGVVKE IDISHHVKEG    50
    FEKADPSQFE LLKVLGQGSY GKVFLVRKVK GSDAGQLYAM KVLKKATLKV 100
    RDRVRSKMER DILAEVNHPF IVKLHYAFQT EGKLYLILDF LRGGDLFTRL 150
    SKEVMFTEED VKFYLAELAL ALDHLHSLGI IYRDLKPENI LLDEEGHIKI 200
    TDFGLSKEAI DHDKRAYSFC GTIEYMAPEV VNRRGHTQSA DWWSFGVLMF 250
    EMLTGSLPFQ GKDRKETMAL ILKAKLGMPQ FLSGEAQSLL RALFKRNPCN 300
    RLGAGIDGVE EIKRHPFFVT IDWNTLYRKE IKPPFKPAVG RPEDTFHFDP 350
    EFTARTPTDS PGVPPSANAH HLFRGFSFVA SSLIQEPSQQ DLHKVPVHPI 400
    VQQLHGNNIH FTDGYEIKED IGVGSYSVCK RCVHKATDTE YAVKIIDKSK 450
    RDPSEEIEIL LRYGQHPNII TLKDVYDDGK FVYLVMELMR GGELLDRILR 500
    QRYFSEREAS DVLCTITKTM DYLHSQGVVH RDLKPSNILY RDESGSPESI 550
    RVCDFGFAKQ LRAGNGLLMT PCYTANFVAP EVLKRQGYDA ACDIWSLGIL 600
    LYTMLAGFTP FANGPDDTPE EILARIGSGK YALSGGNWDS ISDAAKDVVS 650
    KMLHVDPHQR LTAMQVLKHP WVVNREYLSP NQLSRQDVHL VKGAMAATYF 700
    ALNRTPQAPR LEPVLSSNLA QRRGMKRLTS TRL 733
    Length:733
    Mass (Da):83,239
    Last modified:March 21, 2006 - v2
    Checksum:i087CFB819A313760
    GO
    Isoform 2 (identifier: Q15349-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-32: MDLSMKKFAVRRFFSVYLRRKSRSKSSSLSRL → MPIAQLLELW...ACKTKVAGSV

    Note: No experimental confirmation available.

    Show »
    Length:758
    Mass (Da):85,532
    Checksum:i1C30759D0B188D4A
    GO
    Isoform 3 (identifier: Q15349-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-32: MDLSMKKFAVRRFFSVYLRRKSRSKSSSLSRL → MPIAQLLELWKKIEVEPMEIETTEEDLNLDVEPTTEDTAE

    Show »
    Length:741
    Mass (Da):84,014
    Checksum:i146D3569D1C9A193
    GO

    Sequence cautioni

    The sequence BAG53121.1 differs from that shown. Reason: Frameshift at position 527.
    The sequence AAC82496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAD92353.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti256 – 2561S → A in AAC82496. (PubMed:8141249)Curated
    Sequence conflicti269 – 2691A → S in AAC82496. (PubMed:8141249)Curated
    Sequence conflicti339 – 3391V → L in CAA59427. (PubMed:7623830)Curated
    Sequence conflicti339 – 3391V → L in AAC82496. (PubMed:8141249)Curated
    Sequence conflicti447 – 4471D → G in AAC82496. (PubMed:8141249)Curated
    Isoform 3 (identifier: Q15349-3)
    Sequence conflicti32 – 321E → G in BAG53121. (PubMed:14702039)Curated
    Sequence conflicti34 – 341T → A in BAG53121. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti311 – 3111E → K in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_040627
    Natural varianti732 – 7321R → Q in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040628

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3232MDLSM…SLSRL → MPIAQLLELWKKIEVEPMEI ETTEEDLNLDVGPATEDTAE EGKSDSAACKTKVAGSV in isoform 2. 1 PublicationVSP_017732Add
    BLAST
    Alternative sequencei1 – 3232MDLSM…SLSRL → MPIAQLLELWKKIEVEPMEI ETTEEDLNLDVEPTTEDTAE in isoform 3. 1 PublicationVSP_041836Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85106 mRNA. Translation: CAA59427.1.
    AB209116 mRNA. Translation: BAD92353.1. Different initiation.
    AK095751 mRNA. Translation: BAG53121.1. Frameshift.
    AL022069, Z98049 Genomic DNA. Translation: CAI19651.1.
    AL023775 Genomic DNA. No translation available.
    AL159163 Genomic DNA. No translation available.
    Z98049, AL022069 Genomic DNA. Translation: CAI20579.1.
    BC002363 mRNA. Translation: AAH02363.1.
    L07598 mRNA. Translation: AAC82496.1. Different initiation.
    CCDSiCCDS34570.1. [Q15349-3]
    CCDS5294.1. [Q15349-1]
    PIRiA57459.
    RefSeqiNP_001006933.1. NM_001006932.1. [Q15349-3]
    NP_066958.2. NM_021135.4. [Q15349-1]
    UniGeneiHs.655277.

    Genome annotation databases

    EnsembliENST00000265678; ENSP00000265678; ENSG00000071242. [Q15349-1]
    ENST00000503859; ENSP00000427015; ENSG00000071242. [Q15349-3]
    GeneIDi6196.
    KEGGihsa:6196.
    UCSCiuc003qvb.1. human. [Q15349-1]
    uc003qvc.1. human. [Q15349-3]

    Polymorphism databases

    DMDMi90110031.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85106 mRNA. Translation: CAA59427.1 .
    AB209116 mRNA. Translation: BAD92353.1 . Different initiation.
    AK095751 mRNA. Translation: BAG53121.1 . Frameshift.
    AL022069 , Z98049 Genomic DNA. Translation: CAI19651.1 .
    AL023775 Genomic DNA. No translation available.
    AL159163 Genomic DNA. No translation available.
    Z98049 , AL022069 Genomic DNA. Translation: CAI20579.1 .
    BC002363 mRNA. Translation: AAH02363.1 .
    L07598 mRNA. Translation: AAC82496.1 . Different initiation.
    CCDSi CCDS34570.1. [Q15349-3 ]
    CCDS5294.1. [Q15349-1 ]
    PIRi A57459.
    RefSeqi NP_001006933.1. NM_001006932.1. [Q15349-3 ]
    NP_066958.2. NM_021135.4. [Q15349-1 ]
    UniGenei Hs.655277.

    3D structure databases

    ProteinModelPortali Q15349.
    SMRi Q15349. Positions 24-704.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112110. 13 interactions.
    DIPi DIP-295N.
    IntActi Q15349. 11 interactions.
    MINTi MINT-1542928.
    STRINGi 9606.ENSP00000386050.

    Chemistry

    BindingDBi Q15349.
    ChEMBLi CHEMBL3906.
    GuidetoPHARMACOLOGYi 1529.

    PTM databases

    PhosphoSitei Q15349.

    Polymorphism databases

    DMDMi 90110031.

    2D gel databases

    REPRODUCTION-2DPAGE Q15349.

    Proteomic databases

    MaxQBi Q15349.
    PaxDbi Q15349.
    PRIDEi Q15349.

    Protocols and materials databases

    DNASUi 6196.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265678 ; ENSP00000265678 ; ENSG00000071242 . [Q15349-1 ]
    ENST00000503859 ; ENSP00000427015 ; ENSG00000071242 . [Q15349-3 ]
    GeneIDi 6196.
    KEGGi hsa:6196.
    UCSCi uc003qvb.1. human. [Q15349-1 ]
    uc003qvc.1. human. [Q15349-3 ]

    Organism-specific databases

    CTDi 6196.
    GeneCardsi GC06M166822.
    HGNCi HGNC:10431. RPS6KA2.
    HPAi CAB026243.
    HPA045061.
    HPA054237.
    MIMi 601685. gene.
    neXtProti NX_Q15349.
    PharmGKBi PA34846.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    KOi K04373.
    OrthoDBi EOG7B8S38.
    PhylomeDBi Q15349.
    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 Q15349.

    Miscellaneous databases

    ChiTaRSi RPS6KA2. human.
    GeneWikii RPS6KA2.
    GenomeRNAii 6196.
    NextBioi 24063.
    PROi Q15349.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15349.
    Bgeei Q15349.
    CleanExi HS_RPS6KA2.
    Genevestigatori Q15349.

    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. "RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation."
      Zhao Y., Bjoerbaek C., Weremowicz S., Morton C.C., Moller D.E.
      Mol. Cell. Biol. 15:4353-4363(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    2. 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).
      Tissue: Brain.
    3. "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 3).
      Tissue: Brain.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      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: Muscle.
    6. "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] OF 1-540 (ISOFORM 1).
    7. "90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1."
      Jensen C.J., Buch M.-B., Krag T.O., Hemmings B.A., Gammeltoft S., Froedin M.
      J. Biol. Chem. 274:27168-27176(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-218.
    8. "RPS6KA2, a putative tumour suppressor gene at 6q27 in sporadic epithelial ovarian cancer."
      Bignone P.A., Lee K.Y., Liu Y., Emilion G., Finch J., Soosay A.E., Charnock F.M., Beck S., Dunham I., Mungall A.J., Ganesan T.S.
      Oncogene 26:683-700(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TUMORIGENESIS, TISSUE SPECIFICITY.
    9. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-630.
      Tissue: Mammary cancer.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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] LYS-311 AND GLN-732.

    Entry informationi

    Entry nameiKS6A2_HUMAN
    AccessioniPrimary (citable) accession number: Q15349
    Secondary accession number(s): B3KTK9
    , Q15419, Q59GJ3, Q5TI68, Q96J38, Q9UJN5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 152 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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