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Q64702

- PLK4_MOUSE

UniProt

Q64702 - PLK4_MOUSE

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Protein

Serine/threonine-protein kinase PLK4

Gene
Plk4, Sak, Stk18
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 411ATP By similarity
Active sitei136 – 1361Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 269ATP By similarity

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
Complete GO annotation...

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 1 Publication, 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.4 Publications

GO - Cellular componenti

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

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 – 4001Phosphoserine By similarity
Modified residuei778 – 7781Phosphoserine By 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.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiQ64702.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 265254Protein kinaseAdd
BLAST
Domaini847 – 91165POLO boxAdd
BLAST

Sequence similaritiesi

Contains 1 POLO box domain.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei417 – 46448SSNHH…HTVSP → RYSPTKSNVNVLTSLNTKQP IVKDLLKDRIMTEQYKDNLL NLLNKFDR in isoform 2. VSP_011369Add
BLAST
Alternative sequencei465 – 925461Missing in isoform 2. VSP_011370Add
BLAST
Alternative sequencei580 – 60627Missing in isoform 3. VSP_011371Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 123 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

Similar proteinsi