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Q64702

- PLK4_MOUSE

UniProt

Q64702 - PLK4_MOUSE

Protein

Serine/threonine-protein kinase PLK4

Gene

Plk4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      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. Phosphorylates CDC25C and CHEK2. 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 HAND1.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411ATPPROSITE-ProRule annotation
    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. identical protein binding Source: IntAct
    3. protein binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB
    5. protein tyrosine kinase activity Source: InterPro

    GO - Biological processi

    1. centriole replication Source: UniProtKB
    2. de novo centriole assembly Source: UniProtKB
    3. positive regulation of centriole replication Source: UniProtKB
    4. 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. 3474.
    ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:101783. Plk4.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Nucleusnucleolus. Cleavage furrow
    Note: Associates with centrioles throughout the cell cycle. According to PubMed:11301255, it localizes to the nucleolus during G2, to the centrosomes in G2/M, and to the cleavage furrow during cytokinesis. Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles.

    GO - Cellular componenti

    1. centriole Source: UniProtKB
    2. cleavage furrow Source: UniProtKB-SubCell
    3. deuterosome Source: UniProtKB
    4. nucleolus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Death during embryogenesis. Embryos arrest after gastrulation at E7.5, with a marked increase in mitotic and apoptotic cells. Heterozygous mice are viable but show increased liver and lung cancers in elderly mice. Defects in heterozygous mice are associated with progressive cell cycle delays, increased spindle irregularities and accelerated hepatocellular carcinogenesis, probably due to increased centrosomal amplification, multipolar spindle formation and aneuploidy. The incidence of spontaneous.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi170 – 1701T → D: Activating mutant. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 925925Serine/threonine-protein kinase PLK4PRO_0000086568Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei400 – 4001PhosphoserineBy similarity
    Modified residuei778 – 7781PhosphoserineBy similarity

    Post-translational modificationi

    Ubiquitinated; leading to its degradation by the proteasome.1 Publication
    Tyrosine-phosphorylated by TEC.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ64702.

    PTM databases

    PhosphoSiteiQ64702.

    Expressioni

    Tissue specificityi

    expressed in tissues associated with mitotic and meiotic cell division. Highly expressed in testis.1 Publication

    Gene expression databases

    ArrayExpressiQ64702.
    BgeeiQ64702.
    CleanExiMM_PLK4.
    GenevestigatoriQ64702.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-2552433,EBI-2552433
    P037722EBI-2552433,EBI-4478820From a different organism.
    CCNB3Q8WWL74EBI-2552433,EBI-767764From a different organism.
    MBPP02686-12EBI-2552433,EBI-7056012From a different organism.

    Protein-protein interaction databases

    BioGridi203545. 5 interactions.
    IntActiQ64702. 6 interactions.
    MINTiMINT-1341538.

    Structurei

    Secondary structure

    1
    925
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi848 – 8558
    Beta strandi857 – 86610
    Beta strandi871 – 88414
    Beta strandi890 – 8945
    Helixi901 – 9077
    Turni908 – 9103
    Beta strandi913 – 9175

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MBYX-ray2.00A/B839-925[»]
    ProteinModelPortaliQ64702.
    SMRiQ64702. Positions 4-297, 554-768, 845-919.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ64702.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 265254Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini847 – 91165POLO 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.
    GeneTreeiENSGT00530000062954.
    HOVERGENiHBG053617.
    InParanoidiQ80UT6.
    KOiK08863.
    OMAiECASEGY.
    OrthoDBiEOG7NCV33.
    PhylomeDBiQ64702.
    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: Q64702-1) [UniParc]FASTAAdd to Basket

    Also known as: Sak-a

    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

    MAACIGERIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK    50
    AGMVQRVQNE VKIHCQLKHP SVLELYNYFE DNNYVYLVLE MCHNGEMNRY 100
    LKNRMKPFSE REARHFMHQI ITGMLYLHSH GILHRDLTLS NILLTRNMNI 150
    KIADFGLATQ LNMPHEKHYT LCGTPNYISP EIATRSAHGL ESDIWSLGCM 200
    FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PAFLSREAQD LIHQLLRRNP 250
    ADRLSLSSVL DHPFMSRNPS PKSKDVGTVE DSMDSGHATL STTITASSGT 300
    SLSGSLLDRR LLVGQPLPNK ITVFQKNKNS SDFSSGDGSN FCTQWGNPEQ 350
    EANSRGRGRV IEDAEERPHS RYLRRAHSSD RASPSNQSRA KTYSVERCHS 400
    VEMLSKPRRS LDENQHSSNH HCLGKTPFPF ADQTPQMEMV QQWFGNLQMN 450
    AHLGETNEHH TVSPNRDFQD YPDLQDTLRN AWTDTRASKN ADTSANVHAV 500
    KQLSAMKYMS AHHHKPEVMP QEPGLHPHSE QSKNRSMEST LGYQKPTLRS 550
    ITSPLIAHRL KPIRQKTKKA VVSILDSEEV CVELLRECAS EGYVKEVLQI 600
    SSDGTMITVY YPNDGRGFPL ADRPPLPTDN ISRYSFDNLP EKYWRKYQYA 650
    SRFIQLVRSK TPKITYFTRY AKCILMENSP GADFEVWFYD GAKIHKTENL 700
    IHIIEKTGIS YNLKNENEVT SLKEEVKVYM DHANEGHRIC LSLESVISEE 750
    EKRSRGSSFF PIIVGRKPGN TSSPKALSAP PVDPSCCKGE QASASRLSVN 800
    SAAFPTQSPG LSPSTVTVEG LGHTATATGT GVSSSLPKSA QLLKSVFVKN 850
    VGWATQLTSG AVWVQFNDGS QLVVQAGVSS ISYTSPDGQT TRYGENEKLP 900
    EYIKQKLQCL SSILLMFSNP TPNFQ 925
    Length:925
    Mass (Da):103,746
    Last modified:August 16, 2004 - v2
    Checksum:iF28A64ED24D9C801
    GO
    Isoform 2 (identifier: Q64702-2) [UniParc]FASTAAdd to Basket

    Also known as: Sak-b

    The sequence of this isoform differs from the canonical sequence as follows:
         417-464: SSNHHCLGKT...ETNEHHTVSP → RYSPTKSNVN...LLNLLNKFDR
         465-925: Missing.

    Show »
    Length:464
    Mass (Da):52,718
    Checksum:iBA676E303B37B55D
    GO
    Isoform 3 (identifier: Q64702-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         580-606: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:898
    Mass (Da):100,805
    Checksum:iC1FAAD17EE21A142
    GO

    Sequence cautioni

    The sequence AAH51483.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti201 – 2011F → S in AAC37648. (PubMed:8022793)Curated
    Sequence conflicti201 – 2011F → S in AAC37649. (PubMed:8022793)Curated
    Sequence conflicti284 – 2841D → E in BAB24759. (PubMed:16141072)Curated
    Sequence conflicti509 – 5091M → V in BAB24599. (PubMed:16141072)Curated
    Sequence conflicti524 – 5241G → D in AAH26785. 1 PublicationCurated
    Sequence conflicti524 – 5241G → D in AAH57940. 1 PublicationCurated
    Sequence conflicti589 – 5891A → E in AAH26785. 1 PublicationCurated
    Sequence conflicti629 – 6291D → N in AAH26785. 1 PublicationCurated
    Sequence conflicti629 – 6291D → N in AAH57940. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei417 – 46448SSNHH…HTVSP → RYSPTKSNVNVLTSLNTKQP IVKDLLKDRIMTEQYKDNLL NLLNKFDR in isoform 2. 1 PublicationVSP_011369Add
    BLAST
    Alternative sequencei465 – 925461Missing in isoform 2. 1 PublicationVSP_011370Add
    BLAST
    Alternative sequencei580 – 60627Missing in isoform 3. 1 PublicationVSP_011371Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29479 mRNA. Translation: AAC37648.1.
    L29480 mRNA. Translation: AAC37649.1.
    AK006459 mRNA. Translation: BAB24599.1.
    AK006827 mRNA. Translation: BAB24759.1.
    AK137080 mRNA. Translation: BAE23231.1.
    AK137471 mRNA. Translation: BAE23367.1.
    CH466530 Genomic DNA. Translation: EDL35140.1.
    CH466530 Genomic DNA. Translation: EDL35142.1.
    BC026785 mRNA. Translation: AAH26785.1.
    BC051483 mRNA. Translation: AAH51483.1. Different initiation.
    BC057940 mRNA. Translation: AAH57940.1.
    CCDSiCCDS17328.1. [Q64702-1]
    CCDS57210.1. [Q64702-3]
    PIRiA55748.
    RefSeqiNP_035625.2. NM_011495.2. [Q64702-1]
    NP_775261.2. NM_173169.2. [Q64702-3]
    UniGeneiMm.3794.

    Genome annotation databases

    EnsembliENSMUST00000026858; ENSMUSP00000026858; ENSMUSG00000025758. [Q64702-1]
    ENSMUST00000168287; ENSMUSP00000129134; ENSMUSG00000025758. [Q64702-3]
    ENSMUST00000170825; ENSMUSP00000128916; ENSMUSG00000025758. [Q64702-2]
    GeneIDi20873.
    KEGGimmu:20873.
    UCSCiuc008pbm.1. mouse. [Q64702-2]
    uc008pbo.1. mouse. [Q64702-1]
    uc012cpc.1. mouse. [Q64702-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29479 mRNA. Translation: AAC37648.1 .
    L29480 mRNA. Translation: AAC37649.1 .
    AK006459 mRNA. Translation: BAB24599.1 .
    AK006827 mRNA. Translation: BAB24759.1 .
    AK137080 mRNA. Translation: BAE23231.1 .
    AK137471 mRNA. Translation: BAE23367.1 .
    CH466530 Genomic DNA. Translation: EDL35140.1 .
    CH466530 Genomic DNA. Translation: EDL35142.1 .
    BC026785 mRNA. Translation: AAH26785.1 .
    BC051483 mRNA. Translation: AAH51483.1 . Different initiation.
    BC057940 mRNA. Translation: AAH57940.1 .
    CCDSi CCDS17328.1. [Q64702-1 ]
    CCDS57210.1. [Q64702-3 ]
    PIRi A55748.
    RefSeqi NP_035625.2. NM_011495.2. [Q64702-1 ]
    NP_775261.2. NM_173169.2. [Q64702-3 ]
    UniGenei Mm.3794.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MBY X-ray 2.00 A/B 839-925 [» ]
    ProteinModelPortali Q64702.
    SMRi Q64702. Positions 4-297, 554-768, 845-919.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203545. 5 interactions.
    IntActi Q64702. 6 interactions.
    MINTi MINT-1341538.

    PTM databases

    PhosphoSitei Q64702.

    Proteomic databases

    PRIDEi Q64702.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026858 ; ENSMUSP00000026858 ; ENSMUSG00000025758 . [Q64702-1 ]
    ENSMUST00000168287 ; ENSMUSP00000129134 ; ENSMUSG00000025758 . [Q64702-3 ]
    ENSMUST00000170825 ; ENSMUSP00000128916 ; ENSMUSG00000025758 . [Q64702-2 ]
    GeneIDi 20873.
    KEGGi mmu:20873.
    UCSCi uc008pbm.1. mouse. [Q64702-2 ]
    uc008pbo.1. mouse. [Q64702-1 ]
    uc012cpc.1. mouse. [Q64702-3 ]

    Organism-specific databases

    CTDi 10733.
    MGIi MGI:101783. Plk4.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00530000062954.
    HOVERGENi HBG053617.
    InParanoidi Q80UT6.
    KOi K08863.
    OMAi ECASEGY.
    OrthoDBi EOG7NCV33.
    PhylomeDBi Q64702.
    TreeFami TF101090.

    Enzyme and pathway databases

    BRENDAi 2.7.11.21. 3474.
    Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    EvolutionaryTracei Q64702.
    NextBioi 299719.
    PROi Q64702.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q64702.
    Bgeei Q64702.
    CleanExi MM_PLK4.
    Genevestigatori Q64702.

    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. "Sak, a murine protein-serine/threonine kinase that is related to the Drosophila polo kinase and involved in cell proliferation."
      Fode C., Motro B., Yousefi S., Heffernan M., Dennis J.W.
      Proc. Natl. Acad. Sci. U.S.A. 91:6388-6392(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
      Strain: DBA/2.
      Tissue: Lymphoma.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Bone, Embryo and Testis.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 3).
      Strain: FVB/N.
      Tissue: Mammary tumor.
    5. "Constitutive expression of murine Sak-a suppresses cell growth and induces multinucleation."
      Fode C., Binkert C., Dennis J.W.
      Mol. Cell. Biol. 16:4665-4672(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    6. Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    7. "Plk4 haploinsufficiency causes mitotic infidelity and carcinogenesis."
      Ko M.A., Rosario C.O., Hudson J.W., Kulkarni S., Pollett A., Dennis J.W., Swallow C.J.
      Nat. Genet. 37:883-888(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    8. Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-170.
    9. "The Cep63 paralogue Deup1 enables massive de novo centriole biogenesis for vertebrate multiciliogenesis."
      Zhao H., Zhu L., Zhu Y., Cao J., Li S., Huang Q., Xu T., Huang X., Yan X., Zhu X.
      Nat. Cell Biol. 15:1434-1444(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "The Sak polo-box comprises a structural domain sufficient for mitotic subcellular localization."
      Leung G.C., Hudson J.W., Kozarova A., Davidson A., Dennis J.W., Sicheri F.
      Nat. Struct. Biol. 9:719-724(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 839-925, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiPLK4_MOUSE
    AccessioniPrimary (citable) accession number: Q64702
    Secondary accession number(s): Q3UVA3
    , Q6PEP6, Q78EG6, Q80UT6, Q8R0I5, Q9CVR6, Q9CVU6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3