Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UBS0

- KS6B2_HUMAN

UniProt

Q9UBS0 - KS6B2_HUMAN

Protein

Ribosomal protein S6 kinase beta-2

Gene

RPS6KB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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: ProtInc
    4. protein serine/threonine kinase activity Source: ProtInc
    5. ribosomal protein S6 kinase activity Source: Ensembl

    GO - Biological processi

    1. epidermal growth factor receptor signaling pathway Source: Reactome
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. innate immune response Source: Reactome
    5. neurotrophin TRK receptor signaling pathway Source: Reactome
    6. phosphatidylinositol-mediated signaling Source: Reactome
    7. positive regulation of translational initiation Source: UniProtKB
    8. protein kinase B signaling Source: Ensembl
    9. signal transduction Source: ProtInc
    10. translation Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_12442. AKT phosphorylates targets in the nucleus.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    SignaLinkiQ9UBS0.

    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
    Short name:
    P70S6K2
    Short name:
    p70-S6K 2
    S6 kinase-related kinase
    Short name:
    SRK
    Serine/threonine-protein kinase 14B
    p70 ribosomal S6 kinase beta
    Short name:
    S6K-beta
    Short name:
    p70 S6 kinase beta
    Short name:
    p70 S6K-beta
    Short name:
    p70 S6KB
    Short name:
    p70-beta
    Gene namesi
    Name:RPS6KB2
    Synonyms:STK14B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:10437. RPS6KB2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34852.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 482482Ribosomal protein S6 kinase beta-2PRO_0000086214Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151Phosphoserine2 Publications
    Modified residuei423 – 4231PhosphoserineBy similarity
    Modified residuei473 – 4731Phosphoserine; by PKC2 Publications

    Post-translational modificationi

    Phosphorylated and activated by MTOR. Phosphorylation by PKC within the NLS in response to mitogenic stimuli causes cytoplasmic retention.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UBS0.
    PaxDbiQ9UBS0.
    PRIDEiQ9UBS0.

    PTM databases

    PhosphoSiteiQ9UBS0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UBS0.
    BgeeiQ9UBS0.
    CleanExiHS_RPS6KB2.
    GenevestigatoriQ9UBS0.

    Organism-specific databases

    HPAiCAB019404.
    HPA010010.

    Interactioni

    Protein-protein interaction databases

    BioGridi112113. 16 interactions.
    IntActiQ9UBS0. 7 interactions.
    MINTiMINT-207158.
    STRINGi9606.ENSP00000308413.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UBS0.
    SMRiQ9UBS0. 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
    Motifi471 – 4777Nuclear localization signal1 Publication

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi411 – 48272Pro-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiQ9UBS0.
    KOiK04688.
    OMAiLEPAGHY.
    PhylomeDBiQ9UBS0.
    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 splicing. Align

    Isoform 1 (identifier: Q9UBS0-1) [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

    MAAVFDLDLE TEEGSEGEGE PELSPADACP LAELRAAGLE PVGHYEEVEL    50
    TETSVNVGPE RIGPHCFELL RVLGKGGYGK VFQVRKVQGT NLGKIYAMKV 100
    LRKAKIVRNA KDTAHTRAER NILESVKHPF IVELAYAFQT GGKLYLILEC 150
    LSGGELFTHL EREGIFLEDT ACFYLAEITL ALGHLHSQGI IYRDLKPENI 200
    MLSSQGHIKL TDFGLCKESI HEGAVTHTFC GTIEYMAPEI LVRSGHNRAV 250
    DWWSLGALMY DMLTGSPPFT AENRKKTMDK IIRGKLALPP YLTPDARDLV 300
    KKFLKRNPSQ RIGGGPGDAA DVQRHPFFRH MNWDDLLAWR VDPPFRPCLQ 350
    SEEDVSQFDT RFTRQTPVDS PDDTALSESA NQAFLGFTYV APSVLDSIKE 400
    GFSFQPKLRS PRRLNSSPRA PVSPLKFSPF EGFRPSPSLP EPTELPLPPL 450
    LPPPPPSTTA PLPIRPPSGT KKSKRGRGRP GR 482
    Length:482
    Mass (Da):53,455
    Last modified:May 18, 2010 - v2
    Checksum:i5D33660D24A2C7BE
    GO
    Isoform 2 (identifier: Q9UBS0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-154: GG → VD
         155-482: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:154
    Mass (Da):16,868
    Checksum:iB556CDA0AE062FBC
    GO

    Sequence cautioni

    The sequence BAA34402.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901Missing in BAA37145. (PubMed:9878560)Curated
    Sequence conflicti409 – 4091R → C in BAA37145. (PubMed:9878560)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti267 – 2671P → L.1 Publication
    Corresponds to variant rs55987642 [ dbSNP | Ensembl ].
    VAR_040643
    Natural varianti368 – 3681V → M.1 Publication
    Corresponds to variant rs55642995 [ dbSNP | Ensembl ].
    VAR_040644
    Natural varianti420 – 4201A → V.5 Publications
    Corresponds to variant rs13859 [ dbSNP | Ensembl ].
    VAR_040645
    Natural varianti443 – 4431T → M in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_040646

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei153 – 1542GG → VD in isoform 2. 1 PublicationVSP_056441
    Alternative sequencei155 – 482328Missing in isoform 2. 1 PublicationVSP_056442Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB016869 mRNA. Translation: BAA34402.1. Different initiation.
    AB019245 mRNA. Translation: BAA37145.1.
    AF076931 mRNA. Translation: AAD46063.1.
    AF099739 mRNA. Translation: AAD20990.1.
    AK297527 mRNA. Translation: BAG59930.1.
    AP003419 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74621.1.
    BC000094 mRNA. Translation: AAH00094.3.
    BC136564 mRNA. Translation: AAI36565.1.
    CCDSiCCDS41677.1.
    PIRiJE0377.
    RefSeqiNP_003943.2. NM_003952.2.
    UniGeneiHs.534345.

    Genome annotation databases

    EnsembliENST00000312629; ENSP00000308413; ENSG00000175634.
    ENST00000528964; ENSP00000432847; ENSG00000175634.
    GeneIDi6199.
    KEGGihsa:6199.
    UCSCiuc001old.3. human.

    Polymorphism databases

    DMDMi296434560.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB016869 mRNA. Translation: BAA34402.1 . Different initiation.
    AB019245 mRNA. Translation: BAA37145.1 .
    AF076931 mRNA. Translation: AAD46063.1 .
    AF099739 mRNA. Translation: AAD20990.1 .
    AK297527 mRNA. Translation: BAG59930.1 .
    AP003419 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74621.1 .
    BC000094 mRNA. Translation: AAH00094.3 .
    BC136564 mRNA. Translation: AAI36565.1 .
    CCDSi CCDS41677.1.
    PIRi JE0377.
    RefSeqi NP_003943.2. NM_003952.2.
    UniGenei Hs.534345.

    3D structure databases

    ProteinModelPortali Q9UBS0.
    SMRi Q9UBS0. Positions 58-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112113. 16 interactions.
    IntActi Q9UBS0. 7 interactions.
    MINTi MINT-207158.
    STRINGi 9606.ENSP00000308413.

    Chemistry

    ChEMBLi CHEMBL2111330.
    GuidetoPHARMACOLOGYi 1526.

    PTM databases

    PhosphoSitei Q9UBS0.

    Polymorphism databases

    DMDMi 296434560.

    Proteomic databases

    MaxQBi Q9UBS0.
    PaxDbi Q9UBS0.
    PRIDEi Q9UBS0.

    Protocols and materials databases

    DNASUi 6199.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312629 ; ENSP00000308413 ; ENSG00000175634 .
    ENST00000528964 ; ENSP00000432847 ; ENSG00000175634 .
    GeneIDi 6199.
    KEGGi hsa:6199.
    UCSCi uc001old.3. human.

    Organism-specific databases

    CTDi 6199.
    GeneCardsi GC11P067195.
    H-InvDB HIX0009859.
    HGNCi HGNC:10437. RPS6KB2.
    HPAi CAB019404.
    HPA010010.
    MIMi 608939. gene.
    neXtProti NX_Q9UBS0.
    PharmGKBi PA34852.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi Q9UBS0.
    KOi K04688.
    OMAi LEPAGHY.
    PhylomeDBi Q9UBS0.
    TreeFami TF313438.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_12442. AKT phosphorylates targets in the nucleus.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    SignaLinki Q9UBS0.

    Miscellaneous databases

    GeneWikii RPS6KB2.
    GenomeRNAii 6199.
    NextBioi 24077.
    PROi Q9UBS0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBS0.
    Bgeei Q9UBS0.
    CleanExi HS_RPS6KB2.
    Genevestigatori Q9UBS0.

    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. "Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6 kinase beta containing a proline-rich region."
      Gout I., Minami T., Hara K., Tsujishita Y., Filonenko V., Waterfield M.D., Yonezawa K.
      J. Biol. Chem. 273:30061-30064(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-420.
    2. "Cloning and characterization of p70 S6Kbeta defines a novel family of p70 S6 kinases."
      Saitoh M., ten Dijke P., Miyazono K., Ichijo H.
      Biochem. Biophys. Res. Commun. 253:470-476(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-420.
    3. "Characterization of S6K2, a novel kinase homologous to S6K1."
      Lee-Fruman K.K., Kuo C.J., Lippincott J., Terada N., Blenis J.
      Oncogene 18:5108-5114(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-420.
    4. "Cloning and characterization of a novel S6 kinase-related kinase, SRK."
      Koh H.J., Lee B.N., Choi H.S., Chung J.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "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 2).
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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), VARIANT VAL-420.
      Tissue: Brain.
    9. "Regulation of ribosomal S6 kinase 2 by mammalian target of rapamycin."
      Park I.H., Bachmann R., Shirazi H., Chen J.
      J. Biol. Chem. 277:31423-31429(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MTOR, SUBCELLULAR LOCATION.
    10. "Protein kinase C phosphorylates ribosomal protein S6 kinase betaII and regulates its subcellular localization."
      Valovka T., Verdier F., Cramer R., Zhyvoloup A., Fenton T., Rebholz H., Wang M.L., Gzhegotsky M., Lutsyk A., Matsuka G., Filonenko V., Wang L., Proud C.G., Parker P.J., Gout I.T.
      Mol. Cell. Biol. 23:852-863(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-473, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-267; MET-368; VAL-420 AND MET-443.

    Entry informationi

    Entry nameiKS6B2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBS0
    Secondary accession number(s): B2RMZ9
    , B4DML8, O94809, Q9UEC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 147 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 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