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Protein

Serine/threonine-protein kinase PLK4

Gene

Plk4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 – 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 serine/threonine kinase activity Source: UniProtKB

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_272448. Recruitment of mitotic centrosome proteins and complexes.
REACT_276302. Loss of Nlp from mitotic centrosomes.
REACT_286537. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_328862. Anchoring of the basal body to the plasma membrane.
REACT_345278. 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 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:101783. Plk4.

Subcellular locationi

  1. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole
  2. Nucleusnucleolus
  3. Cleavage furrow

  4. 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. centrosome Source: MGI
  3. cleavage furrow Source: UniProtKB-SubCell
  4. deuterosome Source: UniProtKB
  5. nucleolus Source: UniProtKB
  6. XY body Source: MGI
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 – 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

BgeeiQ64702.
CleanExiMM_PLK4.
ExpressionAtlasiQ64702. baseline and differential.
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.
DIPiDIP-42244N.
IntActiQ64702. 6 interactions.
MINTiMINT-1341538.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MBYX-ray2.00A/B839-925[»]
ProteinModelPortaliQ64702.
SMRiQ64702. Positions 4-297, 547-768, 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.
InParanoidiQ64702.
KOiK08863.
OMAiNIVSYER.
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.
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. AlignAdd to basket

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

        10         20         30         40         50
MAACIGERIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK
60 70 80 90 100
AGMVQRVQNE VKIHCQLKHP SVLELYNYFE DNNYVYLVLE MCHNGEMNRY
110 120 130 140 150
LKNRMKPFSE REARHFMHQI ITGMLYLHSH GILHRDLTLS NILLTRNMNI
160 170 180 190 200
KIADFGLATQ LNMPHEKHYT LCGTPNYISP EIATRSAHGL ESDIWSLGCM
210 220 230 240 250
FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PAFLSREAQD LIHQLLRRNP
260 270 280 290 300
ADRLSLSSVL DHPFMSRNPS PKSKDVGTVE DSMDSGHATL STTITASSGT
310 320 330 340 350
SLSGSLLDRR LLVGQPLPNK ITVFQKNKNS SDFSSGDGSN FCTQWGNPEQ
360 370 380 390 400
EANSRGRGRV IEDAEERPHS RYLRRAHSSD RASPSNQSRA KTYSVERCHS
410 420 430 440 450
VEMLSKPRRS LDENQHSSNH HCLGKTPFPF ADQTPQMEMV QQWFGNLQMN
460 470 480 490 500
AHLGETNEHH TVSPNRDFQD YPDLQDTLRN AWTDTRASKN ADTSANVHAV
510 520 530 540 550
KQLSAMKYMS AHHHKPEVMP QEPGLHPHSE QSKNRSMEST LGYQKPTLRS
560 570 580 590 600
ITSPLIAHRL KPIRQKTKKA VVSILDSEEV CVELLRECAS EGYVKEVLQI
610 620 630 640 650
SSDGTMITVY YPNDGRGFPL ADRPPLPTDN ISRYSFDNLP EKYWRKYQYA
660 670 680 690 700
SRFIQLVRSK TPKITYFTRY AKCILMENSP GADFEVWFYD GAKIHKTENL
710 720 730 740 750
IHIIEKTGIS YNLKNENEVT SLKEEVKVYM DHANEGHRIC LSLESVISEE
760 770 780 790 800
EKRSRGSSFF PIIVGRKPGN TSSPKALSAP PVDPSCCKGE QASASRLSVN
810 820 830 840 850
SAAFPTQSPG LSPSTVTVEG LGHTATATGT GVSSSLPKSA QLLKSVFVKN
860 870 880 890 900
VGWATQLTSG AVWVQFNDGS QLVVQAGVSS ISYTSPDGQT TRYGENEKLP
910 920
EYIKQKLQCL SSILLMFSNP TPNFQ
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. Curated

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 (Ref. 3) Curated
Sequence conflicti524 – 5241G → D in AAH57940 (Ref. 3) Curated
Sequence conflicti589 – 5891A → E in AAH26785 (Ref. 3) Curated
Sequence conflicti629 – 6291D → N in AAH26785 (Ref. 3) Curated
Sequence conflicti629 – 6291D → N in AAH57940 (Ref. 3) Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MBYX-ray2.00A/B839-925[»]
ProteinModelPortaliQ64702.
SMRiQ64702. Positions 4-297, 547-768, 845-919.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203545. 5 interactions.
DIPiDIP-42244N.
IntActiQ64702. 6 interactions.
MINTiMINT-1341538.

PTM databases

PhosphoSiteiQ64702.

Proteomic databases

PRIDEiQ64702.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi10733.
MGIiMGI:101783. Plk4.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000062954.
HOVERGENiHBG053617.
InParanoidiQ64702.
KOiK08863.
OMAiNIVSYER.
OrthoDBiEOG7NCV33.
PhylomeDBiQ64702.
TreeFamiTF101090.

Enzyme and pathway databases

BRENDAi2.7.11.21. 3474.
ReactomeiREACT_272448. Recruitment of mitotic centrosome proteins and complexes.
REACT_276302. Loss of Nlp from mitotic centrosomes.
REACT_286537. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_328862. Anchoring of the basal body to the plasma membrane.
REACT_345278. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

EvolutionaryTraceiQ64702.
NextBioi299719.
PROiQ64702.
SOURCEiSearch...

Gene expression databases

BgeeiQ64702.
CleanExiMM_PLK4.
ExpressionAtlasiQ64702. baseline and differential.
GenevestigatoriQ64702.

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.
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]
ProtoNetiSearch...

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: April 29, 2015
This is version 131 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.