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O00444

- PLK4_HUMAN

UniProt

O00444 - PLK4_HUMAN

Protein

Serine/threonine-protein kinase PLK4

Gene

PLK4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2.6 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411ATPCurated
    Active sitei136 – 1361Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 269ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. centriole replication Source: UniProtKB
    2. de novo centriole assembly Source: UniProtKB
    3. G2/M transition of mitotic cell cycle Source: Reactome
    4. mitotic cell cycle Source: Reactome
    5. positive regulation of centriole replication Source: UniProtKB
    6. protein phosphorylation Source: ProtInc
    7. trophoblast giant cell differentiation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.21. 2681.
    ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    SignaLinkiO00444.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase PLK4 (EC:2.7.11.21)
    Alternative name(s):
    Polo-like kinase 4
    Short name:
    PLK-4
    Serine/threonine-protein kinase 18
    Serine/threonine-protein kinase Sak
    Gene namesi
    Name:PLK4
    Synonyms:SAK, STK18
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:11397. PLK4.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Nucleusnucleolus By similarity. Cleavage furrow
    Note: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Associates with centrioles throughout the cell cycle. According to PubMed:16244668, it is not present at cleavage furrows.

    GO - Cellular componenti

    1. centriole Source: UniProtKB
    2. centrosome Source: UniProtKB
    3. cleavage furrow Source: UniProtKB-SubCell
    4. cytosol Source: Reactome
    5. deuterosome Source: UniProtKB
    6. nucleolus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi41 – 411K → M: Abolishes ability to phosphorylate CDC25C and CHEK2. 2 Publications
    Mutagenesisi154 – 1541D → A: Catalytically inactive mutant that causes some centrosome amplification above background levels when overexpressed. 1 Publication
    Mutagenesisi170 – 1701T → D: Activating mutant. 2 Publications

    Organism-specific databases

    PharmGKBiPA36205.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 970970Serine/threonine-protein kinase PLK4PRO_0000086567Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei401 – 4011Phosphoserine3 Publications
    Modified residuei817 – 8171Phosphoserine2 Publications

    Post-translational modificationi

    Ubiquitinated; leading to its degradation by the proteasome.By similarity
    Tyrosine-phosphorylated by TEC.3 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO00444.
    PRIDEiO00444.

    PTM databases

    PhosphoSiteiO00444.

    Expressioni

    Inductioni

    Down-regulated in HCT 116 colorectal cancer cells, leading to aberrant centrioles composed of disorganized cylindrical microtubules and displaced appendages. Down-regulated by p53/TP53.2 Publications

    Gene expression databases

    ArrayExpressiO00444.
    BgeeiO00444.
    CleanExiHS_PLK4.
    GenevestigatoriO00444.

    Organism-specific databases

    HPAiHPA035026.
    HPA043198.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with CEP152 (via N-terminus).By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SFNP319472EBI-746202,EBI-476295

    Protein-protein interaction databases

    BioGridi115956. 15 interactions.
    DIPiDIP-34467N.
    IntActiO00444. 6 interactions.
    MINTiMINT-1460432.
    STRINGi9606.ENSP00000270861.

    Structurei

    Secondary structure

    1
    970
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 54
    Helixi9 – 113
    Beta strandi12 – 209
    Beta strandi22 – 3110
    Turni32 – 343
    Beta strandi37 – 448
    Helixi45 – 506
    Helixi54 – 6411
    Beta strandi75 – 806
    Beta strandi82 – 909
    Helixi97 – 1026
    Beta strandi104 – 1063
    Helixi110 – 12920
    Helixi139 – 1413
    Beta strandi142 – 1443
    Beta strandi150 – 1523
    Turni158 – 1614
    Helixi193 – 20614
    Helixi217 – 2259
    Helixi236 – 24510
    Helixi250 – 2523
    Helixi256 – 2594
    Turni263 – 2653

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3COKX-ray2.25A/B2-275[»]
    4JXFX-ray2.40A4-269[»]
    ProteinModelPortaliO00444.
    SMRiO00444. Positions 4-319, 593-807, 890-964.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00444.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 265254Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini892 – 95665POLO boxPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.PROSITE-ProRule annotation
    Contains 1 POLO box domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG053617.
    InParanoidiO00444.
    KOiK08863.
    OMAiMERCHSA.
    OrthoDBiEOG7NCV33.
    PhylomeDBiO00444.
    TreeFamiTF101090.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000959. POLO_box_duplicated_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008266. Tyr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    PF00659. POLO_box. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50078. POLO_BOX. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00444-1) [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

    MATCIGEKIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK    50
    AGMVQRVQNE VKIHCQLKHP SILELYNYFE DSNYVYLVLE MCHNGEMNRY 100
    LKNRVKPFSE NEARHFMHQI ITGMLYLHSH GILHRDLTLS NLLLTRNMNI 150
    KIADFGLATQ LKMPHEKHYT LCGTPNYISP EIATRSAHGL ESDVWSLGCM 200
    FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PSFLSIEAKD LIHQLLRRNP 250
    ADRLSLSSVL DHPFMSRNSS TKSKDLGTVE DSIDSGHATI STAITASSST 300
    SISGSLFDKR RLLIGQPLPN KMTVFPKNKS STDFSSSGDG NSFYTQWGNQ 350
    ETSNSGRGRV IQDAEERPHS RYLRRAYSSD RSGTSNSQSQ AKTYTMERCH 400
    SAEMLSVSKR SGGGENEERY SPTDNNANIF NFFKEKTSSS SGSFERPDNN 450
    QALSNHLCPG KTPFPFADPT PQTETVQQWF GNLQINAHLR KTTEYDSISP 500
    NRDFQGHPDL QKDTSKNAWT DTKVKKNSDA SDNAHSVKQQ NTMKYMTALH 550
    SKPEIIQQEC VFGSDPLSEQ SKTRGMEPPW GYQNRTLRSI TSPLVAHRLK 600
    PIRQKTKKAV VSILDSEEVC VELVKEYASQ EYVKEVLQIS SDGNTITIYY 650
    PNGGRGFPLA DRPPSPTDNI SRYSFDNLPE KYWRKYQYAS RFVQLVRSKS 700
    PKITYFTRYA KCILMENSPG ADFEVWFYDG VKIHKTEDFI QVIEKTGKSY 750
    TLKSESEVNS LKEEIKMYMD HANEGHRICL ALESIISEEE RKTRSAPFFP 800
    IIIGRKPGST SSPKALSPPP SVDSNYPTRE RASFNRMVMH SAASPTQAPI 850
    LNPSMVTNEG LGLTTTASGT DISSNSLKDC LPKSAQLLKS VFVKNVGWAT 900
    QLTSGAVWVQ FNDGSQLVVQ AGVSSISYTS PNGQTTRYGE NEKLPDYIKQ 950
    KLQCLSSILL MFSNPTPNFH 970
    Length:970
    Mass (Da):108,972
    Last modified:November 13, 2007 - v3
    Checksum:i4D56F5FD983211A6
    GO
    Isoform 2 (identifier: O00444-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         43-74: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:938
    Mass (Da):105,253
    Checksum:i3605FA717C82C2B7
    GO
    Isoform 3 (identifier: O00444-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:929
    Mass (Da):104,636
    Checksum:iECD6808B29B9D8D9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341T → S in BAB69958. (PubMed:11489907)Curated
    Sequence conflicti58 – 581Q → K in CAA73575. 1 PublicationCurated
    Sequence conflicti333 – 3331D → N in BAH13823. (PubMed:14702039)Curated
    Sequence conflicti387 – 3871S → R in BAB69958. (PubMed:11489907)Curated
    Sequence conflicti692 – 6921F → S in BAH13823. (PubMed:14702039)Curated
    Sequence conflicti696 – 6961V → L in BAB69958. (PubMed:11489907)Curated
    Sequence conflicti768 – 7681Y → F in CAA73575. 1 PublicationCurated
    Sequence conflicti842 – 8421A → D in BAB69958. (PubMed:11489907)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti86 – 861Y → C.1 Publication
    Corresponds to variant rs34156294 [ dbSNP | Ensembl ].
    VAR_041027
    Natural varianti146 – 1461R → H.1 Publication
    Corresponds to variant rs35232579 [ dbSNP | Ensembl ].
    VAR_041028
    Natural varianti226 – 2261A → T.1 Publication
    Corresponds to variant rs35448573 [ dbSNP | Ensembl ].
    VAR_041029
    Natural varianti232 – 2321S → T.4 Publications
    Corresponds to variant rs3811740 [ dbSNP | Ensembl ].
    VAR_019632
    Natural varianti317 – 3171P → L.1 Publication
    Corresponds to variant rs35049837 [ dbSNP | Ensembl ].
    VAR_041030
    Natural varianti449 – 4491N → D.1 Publication
    Corresponds to variant rs34906574 [ dbSNP | Ensembl ].
    VAR_041031
    Natural varianti519 – 5191W → S.1 Publication
    Corresponds to variant rs56043017 [ dbSNP | Ensembl ].
    VAR_041032
    Natural varianti830 – 8301E → D.4 Publications
    Corresponds to variant rs17012739 [ dbSNP | Ensembl ].
    VAR_041033

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4141Missing in isoform 3. 1 PublicationVSP_038116Add
    BLAST
    Alternative sequencei43 – 7432Missing in isoform 2. 1 PublicationVSP_038117Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13115 mRNA. Translation: CAA73575.1.
    AB006972 mRNA. Translation: BAB69958.1.
    AK302858 mRNA. Translation: BAH13823.1.
    AK303399 mRNA. Translation: BAH13953.1.
    AK314238 mRNA. Translation: BAG36907.1.
    BC036023 mRNA. Translation: AAH36023.1.
    CCDSiCCDS3735.1. [O00444-1]
    CCDS54803.1. [O00444-2]
    CCDS54804.1. [O00444-3]
    RefSeqiNP_001177728.1. NM_001190799.1. [O00444-2]
    NP_001177730.1. NM_001190801.1. [O00444-3]
    NP_055079.3. NM_014264.4. [O00444-1]
    UniGeneiHs.172052.

    Genome annotation databases

    EnsembliENST00000270861; ENSP00000270861; ENSG00000142731. [O00444-1]
    ENST00000513090; ENSP00000427554; ENSG00000142731. [O00444-2]
    ENST00000514379; ENSP00000423582; ENSG00000142731. [O00444-3]
    GeneIDi10733.
    KEGGihsa:10733.
    UCSCiuc003ifo.3. human. [O00444-1]
    uc011cgs.2. human. [O00444-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13115 mRNA. Translation: CAA73575.1 .
    AB006972 mRNA. Translation: BAB69958.1 .
    AK302858 mRNA. Translation: BAH13823.1 .
    AK303399 mRNA. Translation: BAH13953.1 .
    AK314238 mRNA. Translation: BAG36907.1 .
    BC036023 mRNA. Translation: AAH36023.1 .
    CCDSi CCDS3735.1. [O00444-1 ]
    CCDS54803.1. [O00444-2 ]
    CCDS54804.1. [O00444-3 ]
    RefSeqi NP_001177728.1. NM_001190799.1. [O00444-2 ]
    NP_001177730.1. NM_001190801.1. [O00444-3 ]
    NP_055079.3. NM_014264.4. [O00444-1 ]
    UniGenei Hs.172052.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3COK X-ray 2.25 A/B 2-275 [» ]
    4JXF X-ray 2.40 A 4-269 [» ]
    ProteinModelPortali O00444.
    SMRi O00444. Positions 4-319, 593-807, 890-964.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115956. 15 interactions.
    DIPi DIP-34467N.
    IntActi O00444. 6 interactions.
    MINTi MINT-1460432.
    STRINGi 9606.ENSP00000270861.

    Chemistry

    BindingDBi O00444.
    ChEMBLi CHEMBL3788.
    GuidetoPHARMACOLOGYi 2171.

    PTM databases

    PhosphoSitei O00444.

    Proteomic databases

    PaxDbi O00444.
    PRIDEi O00444.

    Protocols and materials databases

    DNASUi 10733.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000270861 ; ENSP00000270861 ; ENSG00000142731 . [O00444-1 ]
    ENST00000513090 ; ENSP00000427554 ; ENSG00000142731 . [O00444-2 ]
    ENST00000514379 ; ENSP00000423582 ; ENSG00000142731 . [O00444-3 ]
    GeneIDi 10733.
    KEGGi hsa:10733.
    UCSCi uc003ifo.3. human. [O00444-1 ]
    uc011cgs.2. human. [O00444-2 ]

    Organism-specific databases

    CTDi 10733.
    GeneCardsi GC04P128802.
    HGNCi HGNC:11397. PLK4.
    HPAi HPA035026.
    HPA043198.
    MIMi 605031. gene.
    neXtProti NX_O00444.
    PharmGKBi PA36205.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG053617.
    InParanoidi O00444.
    KOi K08863.
    OMAi MERCHSA.
    OrthoDBi EOG7NCV33.
    PhylomeDBi O00444.
    TreeFami TF101090.

    Enzyme and pathway databases

    BRENDAi 2.7.11.21. 2681.
    Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    SignaLinki O00444.

    Miscellaneous databases

    EvolutionaryTracei O00444.
    GeneWikii PLK4.
    GenomeRNAii 10733.
    NextBioi 40744.
    PROi O00444.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00444.
    Bgeei O00444.
    CleanExi HS_PLK4.
    Genevestigatori O00444.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000959. POLO_box_duplicated_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008266. Tyr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    PF00659. POLO_box. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50078. POLO_BOX. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human SAK related to the PLK/polo family of cell cycle kinases shows high mRNA expression in testis."
      Karn T., Holtrich U., Wolf G., Hock B., Strebhardt K., Ruebsamen-Waigmann H.
      Oncol. Rep. 4:505-510(1997)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-232 AND ASP-830.
      Tissue: Lung.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION BY TEC, VARIANTS THR-232 AND ASP-830.
      Tissue: Blood.
    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] (ISOFORMS 1; 2 AND 3), VARIANTS THR-232 AND ASP-830.
      Tissue: Testis and Thymus.
    4. "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: Testis.
    5. "Transmembrane signaling by the interleukin-2 receptor: progress and conundrums."
      Mills G.B., Schmandt R., Gibson S., Leung B., Hill M., May C., Shi Y.F., Branch D.R., Radvanyi L., Truitt K.E., Imboden J.
      Semin. Immunol. 5:345-364(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 134-196.
    6. "Analysis of tyrosine kinase mRNAs including four FGF receptor mRNAs expressed in MCF-7 breast-cancer cells."
      Lehtola L., Partanen J., Sistonen L., Korhonen J., Warri A., Harkonen P., Clarke R., Alitalo K.
      Int. J. Cancer 50:598-603(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 135-196.
      Tissue: Mammary carcinoma.
    7. Cited for: FUNCTION.
    8. "The Polo kinase Plk4 functions in centriole duplication."
      Habedanck R., Stierhof Y.-D., Wilkinson C.J., Nigg E.A.
      Nat. Cell Biol. 7:1140-1146(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-154.
    9. "SAK, a new polo-like kinase, is transcriptionally repressed by p53 and induces apoptosis upon RNAi silencing."
      Li J., Tan M., Li L., Pamarthy D., Lawrence T.S., Sun Y.
      Neoplasia 7:312-323(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY TP53.
    10. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Human Plk4 phosphorylates Cdc25C."
      Bonni S., Ganuelas M.L., Petrinac S., Hudson J.W.
      Cell Cycle 7:545-547(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-41 AND THR-170.
    12. "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-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Polo-like kinase 4 phosphorylates Chk2."
      Petrinac S., Ganuelas M.L., Bonni S., Nantais J., Hudson J.W.
      Cell Cycle 8:327-329(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-41 AND THR-170.
    15. "Gamma-tubulin-containing abnormal centrioles are induced by insufficient Plk4 in human HCT116 colorectal cancer cells."
      Kuriyama R., Bettencourt-Dias M., Hoffmann I., Arnold M., Sandvig L.
      J. Cell Sci. 122:2014-2023(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Cep152 acts as a scaffold for recruitment of Plk4 and CPAP to the centrosome."
      Cizmecioglu O., Arnold M., Bahtz R., Settele F., Ehret L., Haselmann-Weiss U., Antony C., Hoffmann I.
      J. Cell Biol. 191:731-739(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CEP152.
    18. Cited for: INTERACTION WITH CEP152.
    19. "The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6 to control centrosome duplication."
      Puklowski A., Homsi Y., Keller D., May M., Chauhan S., Kossatz U., Grunwald V., Kubicka S., Pich A., Manns M.P., Hoffmann I., Gonczy P., Malek N.P.
      Nat. Cell Biol. 13:1004-1009(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF FBXW5.
    20. "Crystal structure of PLK4 kinase."
      New York structural genomix research consortium (NYSGXRC)
      Submitted (JUN-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-275.
    21. "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] CYS-86; HIS-146; THR-226; THR-232; LEU-317; ASP-449; SER-519 AND ASP-830.

    Entry informationi

    Entry nameiPLK4_HUMAN
    AccessioniPrimary (citable) accession number: O00444
    Secondary accession number(s): B2RAL0
    , B7Z837, B7Z8G7, Q8IYF0, Q96Q95, Q9UD84, Q9UDE2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 133 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3