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Q96KB5

- TOPK_HUMAN

UniProt

Q96KB5 - TOPK_HUMAN

Protein

Lymphokine-activated killer T-cell-originated protein kinase

Gene

PBK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 3 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Activated by phosphorylation.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei64 – 641ATPPROSITE-ProRule annotation
    Active sitei167 – 1671Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi38 – 469ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ96KB5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lymphokine-activated killer T-cell-originated protein kinase (EC:2.7.12.2)
    Alternative name(s):
    Cancer/testis antigen 84
    Short name:
    CT84
    MAPKK-like protein kinase
    Nori-3
    PDZ-binding kinase
    Spermatogenesis-related protein kinase
    Short name:
    SPK
    T-LAK cell-originated protein kinase
    Gene namesi
    Name:PBK
    Synonyms:TOPK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:18282. PBK.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91T → E: TP53-binding. 1 Publication
    Mutagenesisi64 – 652KK → AA: Loss of activity.
    Mutagenesisi320 – 3201T → A: Decrease in the binding to DLG1. 1 Publication
    Mutagenesisi322 – 3221V → A: Decrease in the binding to DLG1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134925802.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 322322Lymphokine-activated killer T-cell-originated protein kinasePRO_0000086763Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei9 – 91Phosphothreonine1 Publication
    Modified residuei24 – 241Phosphothreonine1 Publication
    Modified residuei32 – 321Phosphoserine2 Publications
    Modified residuei59 – 591Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated; in a cell-cycle dependent manner at mitosis.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96KB5.
    PaxDbiQ96KB5.
    PeptideAtlasiQ96KB5.
    PRIDEiQ96KB5.

    PTM databases

    PhosphoSiteiQ96KB5.

    Expressioni

    Tissue specificityi

    Expressed in the testis and placenta. In the testis, restrictedly expressed in outer cell layer of seminiferous tubules.2 Publications

    Gene expression databases

    ArrayExpressiQ96KB5.
    BgeeiQ96KB5.
    CleanExiHS_PBK.
    GenevestigatoriQ96KB5.

    Organism-specific databases

    HPAiHPA005753.

    Interactioni

    Subunit structurei

    Interacts with DLG1 and TP53.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARAFP103983EBI-536853,EBI-365961
    TP53P046377EBI-536853,EBI-366083

    Protein-protein interaction databases

    BioGridi120971. 14 interactions.
    IntActiQ96KB5. 9 interactions.
    MINTiMINT-130347.
    STRINGi9606.ENSP00000301905.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96KB5.
    SMRiQ96KB5. Positions 34-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 322291Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni320 – 3223PDZ-interaction

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000294208.
    HOVERGENiHBG056011.
    InParanoidiQ96KB5.
    KOiK08865.
    OrthoDBiEOG7S4X6F.
    PhylomeDBiQ96KB5.
    TreeFamiTF329763.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. 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: Q96KB5-1) [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

    MEGISNFKTP SKLSEKKKSV LCSTPTINIP ASPFMQKLGF GTGVNVYLMK    50
    RSPRGLSHSP WAVKKINPIC NDHYRSVYQK RLMDEAKILK SLHHPNIVGY 100
    RAFTEANDGS LCLAMEYGGE KSLNDLIEER YKASQDPFPA AIILKVALNM 150
    ARGLKYLHQE KKLLHGDIKS SNVVIKGDFE TIKICDVGVS LPLDENMTVT 200
    DPEACYIGTE PWKPKEAVEE NGVITDKADI FAFGLTLWEM MTLSIPHINL 250
    SNDDDDEDKT FDESDFDDEA YYAALGTRPP INMEELDESY QKVIELFSVC 300
    TNEDPKDRPS AAHIVEALET DV 322
    Length:322
    Mass (Da):36,085
    Last modified:December 6, 2005 - v3
    Checksum:i6BF55789BC204ABE
    GO
    Isoform 2 (identifier: Q96KB5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         198-198: T → TAPAFITILLVS

    Note: No experimental confirmation available.

    Show »
    Length:333
    Mass (Da):37,211
    Checksum:i05A472E8DD4D9928
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341F → I in AAF71521. (PubMed:11378444)Curated
    Sequence conflicti169 – 1691K → E in BAB55019. (PubMed:14702039)Curated
    Sequence conflicti254 – 2541D → N in BAB55019. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071N → S.4 Publications
    Corresponds to variant rs3779620 [ dbSNP | Ensembl ].
    VAR_021162
    Natural varianti220 – 2201E → D.
    Corresponds to variant rs17057901 [ dbSNP | Ensembl ].
    VAR_051676
    Natural varianti241 – 2411M → L.1 Publication
    Corresponds to variant rs36086402 [ dbSNP | Ensembl ].
    VAR_041234

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei198 – 1981T → TAPAFITILLVS in isoform 2. 1 PublicationVSP_055269

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB027249 mRNA. Translation: BAA99576.1.
    AB027250 mRNA. Translation: BAA99577.1.
    AF189722 mRNA. Translation: AAF69107.1.
    AF237709 mRNA. Translation: AAF71521.1.
    AK027291 mRNA. Translation: BAB55019.1.
    AK301836 mRNA. Translation: BAG63280.1.
    AC104997 Genomic DNA. No translation available.
    CH471080 Genomic DNA. Translation: EAW63536.1.
    CH471080 Genomic DNA. Translation: EAW63537.1.
    BC015191 mRNA. Translation: AAH15191.1.
    CCDSiCCDS6063.1. [Q96KB5-1]
    CCDS64858.1. [Q96KB5-2]
    RefSeqiNP_001265874.1. NM_001278945.1.
    NP_060962.2. NM_018492.3.
    XP_006716431.1. XM_006716368.1.
    UniGeneiHs.104741.

    Genome annotation databases

    EnsembliENST00000301905; ENSP00000301905; ENSG00000168078. [Q96KB5-1]
    ENST00000522944; ENSP00000428489; ENSG00000168078. [Q96KB5-2]
    GeneIDi55872.
    KEGGihsa:55872.
    UCSCiuc003xgi.3. human. [Q96KB5-1]

    Polymorphism databases

    DMDMi83305809.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB027249 mRNA. Translation: BAA99576.1 .
    AB027250 mRNA. Translation: BAA99577.1 .
    AF189722 mRNA. Translation: AAF69107.1 .
    AF237709 mRNA. Translation: AAF71521.1 .
    AK027291 mRNA. Translation: BAB55019.1 .
    AK301836 mRNA. Translation: BAG63280.1 .
    AC104997 Genomic DNA. No translation available.
    CH471080 Genomic DNA. Translation: EAW63536.1 .
    CH471080 Genomic DNA. Translation: EAW63537.1 .
    BC015191 mRNA. Translation: AAH15191.1 .
    CCDSi CCDS6063.1. [Q96KB5-1 ]
    CCDS64858.1. [Q96KB5-2 ]
    RefSeqi NP_001265874.1. NM_001278945.1.
    NP_060962.2. NM_018492.3.
    XP_006716431.1. XM_006716368.1.
    UniGenei Hs.104741.

    3D structure databases

    ProteinModelPortali Q96KB5.
    SMRi Q96KB5. Positions 34-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120971. 14 interactions.
    IntActi Q96KB5. 9 interactions.
    MINTi MINT-130347.
    STRINGi 9606.ENSP00000301905.

    Chemistry

    BindingDBi Q96KB5.
    ChEMBLi CHEMBL4896.
    GuidetoPHARMACOLOGYi 2140.

    PTM databases

    PhosphoSitei Q96KB5.

    Polymorphism databases

    DMDMi 83305809.

    Proteomic databases

    MaxQBi Q96KB5.
    PaxDbi Q96KB5.
    PeptideAtlasi Q96KB5.
    PRIDEi Q96KB5.

    Protocols and materials databases

    DNASUi 55872.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301905 ; ENSP00000301905 ; ENSG00000168078 . [Q96KB5-1 ]
    ENST00000522944 ; ENSP00000428489 ; ENSG00000168078 . [Q96KB5-2 ]
    GeneIDi 55872.
    KEGGi hsa:55872.
    UCSCi uc003xgi.3. human. [Q96KB5-1 ]

    Organism-specific databases

    CTDi 55872.
    GeneCardsi GC08M027724.
    HGNCi HGNC:18282. PBK.
    HPAi HPA005753.
    MIMi 611210. gene.
    neXtProti NX_Q96KB5.
    PharmGKBi PA134925802.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000294208.
    HOVERGENi HBG056011.
    InParanoidi Q96KB5.
    KOi K08865.
    OrthoDBi EOG7S4X6F.
    PhylomeDBi Q96KB5.
    TreeFami TF329763.

    Enzyme and pathway databases

    SignaLinki Q96KB5.

    Miscellaneous databases

    ChiTaRSi PBK. human.
    GeneWikii PBK_(gene).
    GenomeRNAii 55872.
    NextBioi 35475910.
    PROi Q96KB5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96KB5.
    Bgeei Q96KB5.
    CleanExi HS_PBK.
    Genevestigatori Q96KB5.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of a novel MAPKK-like protein kinase, lymphokine-activated killer T-cell-originated protein kinase, specifically expressed in the testis and activated lymphoid cells."
      Abe Y., Matsumoto S., Kito K., Ueda N.
      J. Biol. Chem. 275:21525-21531(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY.
      Tissue: Lymphoid tissue.
    2. "Characterization of PDZ-binding kinase, a mitotic kinase."
      Gaudet S., Branton D., Lue R.A.
      Proc. Natl. Acad. Sci. U.S.A. 97:5167-5172(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, MUTAGENESIS OF 64-LEU-LEU-65; THR-320 AND VAL-322, INTERACTION WITH DLG1, VARIANT SER-107.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-107.
      Tissue: Fetal brain.
    4. "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] (ISOFORMS 1 AND 2), VARIANT SER-107.
      Tissue: Embryo and Testis.
    5. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Brain.
    8. "Attenuation of DNA damage checkpoint by PBK, a novel mitotic kinase, involves protein-protein interaction with tumor suppressor p53."
      Nandi A.K., Ford T., Fleksher D., Neuman B., Rapoport A.P.
      Biochem. Biophys. Res. Commun. 358:181-188(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53, MUTAGENESIS OF THR-9.
    9. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-32 AND SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9; SER-32 AND SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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] SER-107 AND LEU-241.

    Entry informationi

    Entry nameiTOPK_HUMAN
    AccessioniPrimary (citable) accession number: Q96KB5
    Secondary accession number(s): B4DX68
    , D3DST2, Q9NPD9, Q9NYL7, Q9NZK6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 117 of the entry and version 3 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 8
      Human chromosome 8: 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