Q64702 (PLK4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Plk4
Synonyms:	Sak, Stk18

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	925 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Homodimer. Interacts with CEP152 (via N-terminus) By similarity. Ref.9
Subcellular location	Cytoplasm › cytoskeleton › centrosome › centriole. Nucleus › nucleolus. Cleavage furrow. Note: Associates with centrioles throughout the cell cycle. According to Ref.6, it localizes to the nucleolus during G2, to the centrosomes in G2/M, and to the cleavage furrow during cytokinesis. Ref.6 Ref.8 Ref.9
Tissue specificity	expressed in tissues associated with mitotic and meiotic cell division. Highly expressed in testis. Ref.1
Post-translational modification	Ubiquitinated; leading to its degradation by the proteasome. Ref.5 Tyrosine-phosphorylated by TEC By similarity.
Disruption phenotype	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. Ref.6 Ref.7
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily. Contains 1 POLO box domain. Contains 1 protein kinase domain.
Sequence caution	The sequence AAH51483.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	centriole replication Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of centriole replication Inferred from sequence or structural similarity. Source: UniProtKB trophoblast giant cell differentiation Inferred from mutant phenotype Ref.8. Source: UniProtKB
Cellular_component	centriole Inferred from sequence or structural similarity. Source: UniProtKB cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.8. Source: UniProtKB protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q64702-1)

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.

Isoform 2 (identifier: Q64702-2)

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.

Isoform 3 (identifier: Q64702-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 925

925

Serine/threonine-protein kinase PLK4

PRO_0000086568

Regions

Domain

12 – 265

254

Protein kinase

Domain

847 – 911

65

POLO box

Nucleotide binding

18 – 26

9

ATP By similarity

Sites

Active site

136

1

Proton acceptor By similarity

Binding site

41

1

ATP By similarity

Amino acid modifications

Modified residue

400

1

Phosphoserine By similarity

Modified residue

778

1

Phosphoserine By similarity

Natural variations

Alternative sequence

417 – 464

48

SSNHH…HTVSP → RYSPTKSNVNVLTSLNTKQP IVKDLLKDRIMTEQYKDNLL NLLNKFDR in isoform 2.

VSP_011369

Alternative sequence

465 – 925

461

Missing in isoform 2.

VSP_011370

Alternative sequence

580 – 606

27

Missing in isoform 3.

VSP_011371

Experimental info

Mutagenesis

170

1

T → D: Activating mutant. Ref.8

Sequence conflict

201

1

F → S in AAC37648. Ref.1

Sequence conflict

201

1

F → S in AAC37649. Ref.1

Sequence conflict

284

1

D → E in BAB24759. Ref.2

Sequence conflict

509

1

M → V in BAB24599. Ref.2

Sequence conflict

524

1

G → D in AAH26785. Ref.3

Sequence conflict

524

1

G → D in AAH57940. Ref.3

Sequence conflict

589

1

A → E in AAH26785. Ref.3

Sequence conflict

629

1

D → N in AAH26785. Ref.3

Sequence conflict

629

1

D → N in AAH57940. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

925

Helix Strand Turn

Details...

Beta strand

848 – 855

8

Beta strand

857 – 866

10

Beta strand

871 – 884

14

Beta strand

890 – 894

5

Helix

901 – 907

7

Turn

908 – 910

3

Beta strand

913 – 917

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Sak-a) [UniParc]. Last modified August 16, 2004. Version 2. Checksum: F28A64ED24D9C801	FASTA	925	103,746
	10 20 30 40 50 60 MAACIGERIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE 70 80 90 100 110 120 VKIHCQLKHP SVLELYNYFE DNNYVYLVLE MCHNGEMNRY LKNRMKPFSE REARHFMHQI 130 140 150 160 170 180 ITGMLYLHSH GILHRDLTLS NILLTRNMNI KIADFGLATQ LNMPHEKHYT LCGTPNYISP 190 200 210 220 230 240 EIATRSAHGL ESDIWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PAFLSREAQD 250 260 270 280 290 300 LIHQLLRRNP ADRLSLSSVL DHPFMSRNPS PKSKDVGTVE DSMDSGHATL STTITASSGT 310 320 330 340 350 360 SLSGSLLDRR LLVGQPLPNK ITVFQKNKNS SDFSSGDGSN FCTQWGNPEQ EANSRGRGRV 370 380 390 400 410 420 IEDAEERPHS RYLRRAHSSD RASPSNQSRA KTYSVERCHS VEMLSKPRRS LDENQHSSNH 430 440 450 460 470 480 HCLGKTPFPF ADQTPQMEMV QQWFGNLQMN AHLGETNEHH TVSPNRDFQD YPDLQDTLRN 490 500 510 520 530 540 AWTDTRASKN ADTSANVHAV KQLSAMKYMS AHHHKPEVMP QEPGLHPHSE QSKNRSMEST 550 560 570 580 590 600 LGYQKPTLRS ITSPLIAHRL KPIRQKTKKA VVSILDSEEV CVELLRECAS EGYVKEVLQI 610 620 630 640 650 660 SSDGTMITVY YPNDGRGFPL ADRPPLPTDN ISRYSFDNLP EKYWRKYQYA SRFIQLVRSK 670 680 690 700 710 720 TPKITYFTRY AKCILMENSP GADFEVWFYD GAKIHKTENL IHIIEKTGIS YNLKNENEVT 730 740 750 760 770 780 SLKEEVKVYM DHANEGHRIC LSLESVISEE EKRSRGSSFF PIIVGRKPGN TSSPKALSAP 790 800 810 820 830 840 PVDPSCCKGE QASASRLSVN SAAFPTQSPG LSPSTVTVEG LGHTATATGT GVSSSLPKSA 850 860 870 880 890 900 QLLKSVFVKN VGWATQLTSG AVWVQFNDGS QLVVQAGVSS ISYTSPDGQT TRYGENEKLP 910 920 EYIKQKLQCL SSILLMFSNP TPNFQ
	Isoform 2 (Sak-b) [UniParc]. Checksum: BA676E303B37B55D	FASTA	464	52,718
	10 20 30 40 50 60 MAACIGERIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE 70 80 90 100 110 120 VKIHCQLKHP SVLELYNYFE DNNYVYLVLE MCHNGEMNRY LKNRMKPFSE REARHFMHQI 130 140 150 160 170 180 ITGMLYLHSH GILHRDLTLS NILLTRNMNI KIADFGLATQ LNMPHEKHYT LCGTPNYISP 190 200 210 220 230 240 EIATRSAHGL ESDIWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PAFLSREAQD 250 260 270 280 290 300 LIHQLLRRNP ADRLSLSSVL DHPFMSRNPS PKSKDVGTVE DSMDSGHATL STTITASSGT 310 320 330 340 350 360 SLSGSLLDRR LLVGQPLPNK ITVFQKNKNS SDFSSGDGSN FCTQWGNPEQ EANSRGRGRV 370 380 390 400 410 420 IEDAEERPHS RYLRRAHSSD RASPSNQSRA KTYSVERCHS VEMLSKPRRS LDENQHRYSP 430 440 450 460 TKSNVNVLTS LNTKQPIVKD LLKDRIMTEQ YKDNLLNLLN KFDR
	Isoform 3 [UniParc]. Checksum: C1FAAD17EE21A142	FASTA	898	100,805
	10 20 30 40 50 60 MAACIGERIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE 70 80 90 100 110 120 VKIHCQLKHP SVLELYNYFE DNNYVYLVLE MCHNGEMNRY LKNRMKPFSE REARHFMHQI 130 140 150 160 170 180 ITGMLYLHSH GILHRDLTLS NILLTRNMNI KIADFGLATQ LNMPHEKHYT LCGTPNYISP 190 200 210 220 230 240 EIATRSAHGL ESDIWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PAFLSREAQD 250 260 270 280 290 300 LIHQLLRRNP ADRLSLSSVL DHPFMSRNPS PKSKDVGTVE DSMDSGHATL STTITASSGT 310 320 330 340 350 360 SLSGSLLDRR LLVGQPLPNK ITVFQKNKNS SDFSSGDGSN FCTQWGNPEQ EANSRGRGRV 370 380 390 400 410 420 IEDAEERPHS RYLRRAHSSD RASPSNQSRA KTYSVERCHS VEMLSKPRRS LDENQHSSNH 430 440 450 460 470 480 HCLGKTPFPF ADQTPQMEMV QQWFGNLQMN AHLGETNEHH TVSPNRDFQD YPDLQDTLRN 490 500 510 520 530 540 AWTDTRASKN ADTSANVHAV KQLSAMKYMS AHHHKPEVMP QEPGLHPHSE QSKNRSMEST 550 560 570 580 590 600 LGYQKPTLRS ITSPLIAHRL KPIRQKTKKA VVSILDSEEI TVYYPNDGRG FPLADRPPLP 610 620 630 640 650 660 TDNISRYSFD NLPEKYWRKY QYASRFIQLV RSKTPKITYF TRYAKCILME NSPGADFEVW 670 680 690 700 710 720 FYDGAKIHKT ENLIHIIEKT GISYNLKNEN EVTSLKEEVK VYMDHANEGH RICLSLESVI 730 740 750 760 770 780 SEEEKRSRGS SFFPIIVGRK PGNTSSPKAL SAPPVDPSCC KGEQASASRL SVNSAAFPTQ 790 800 810 820 830 840 SPGLSPSTVT VEGLGHTATA TGTGVSSSLP KSAQLLKSVF VKNVGWATQL TSGAVWVQFN 850 860 870 880 890 DGSQLVVQAG VSSISYTSPD GQTTRYGENE KLPEYIKQKL QCLSSILLMF SNPTPNFQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Late mitotic failure in mice lacking Sak, a polo-like kinase." Hudson J.W., Kozarova A., Cheung P., Macmillan J.C., Swallow C.J., Cross J.C., Dennis J.W. Curr. Biol. 11:441-446(2001) [PubMed] [Europe PMC] [Abstract] 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]	"Nucleolar release of Hand1 acts as a molecular switch to determine cell fate." Martindill D.M.J., Risebro C.A., Smart N., Franco-Viseras Mdel M., Rosario C.O., Swallow C.J., Dennis J.W., Riley P.R. Nat. Cell Biol. 9:1131-1141(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-170.
[9]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00457874.
IPI00457875.
IPI00457876.

PIR

A55748.

RefSeq

NP_035625.2. NM_011495.2.
NP_775261.2. NM_173169.2.

UniGene

Mm.3794.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MBY	X-ray	2.00	A/B	839-925	[»]

ProteinModelPortal

Q64702.

SMR

Q64702. Positions 1-309, 554-768, 845-919.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q64702. 3 interactions.

MINT

MINT-1341538.

PTM databases

PhosphoSite

Q64702.

Proteomic databases

PRIDE

Q64702.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000026858; ENSMUSP00000026858; ENSMUSG00000025758.
ENSMUST00000168287; ENSMUSP00000129134; ENSMUSG00000025758.
ENSMUST00000170825; ENSMUSP00000128916; ENSMUSG00000025758.

GeneID

20873.

KEGG

mmu:20873.

UCSC

uc008pbm.1. mouse.
uc008pbo.1. mouse.
uc012cpc.1. mouse.

Organism-specific databases

CTD

10733.

MGI

MGI:101783. Plk4.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00530000062954.

HOVERGEN

HBG053617.

InParanoid

Q80UT6.

KO

K08863.

OMA

NTMERCH.

OrthoDB

EOG4W9J37.

Enzyme and pathway databases

BRENDA

2.7.11.21. 3474.

Gene expression databases

ArrayExpress

Q64702.

Bgee

Q64702.

CleanEx

MM_PLK4.

Genevestigator

Q64702.

GermOnline

ENSMUSG00000025758. Mus musculus.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000959. POLO_box_duplicated_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
PF00659. POLO_box. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50078. POLO_BOX. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q64702.

NextBio

299719.

SOURCE

Search...

Entry information

Entry name

PLK4_MOUSE

Accession

Primary (citable) accession number: Q64702
Secondary accession number(s): Q3UVA3 , Q6PEP6, Q78EG6, Q80UT6, Q8R0I5, Q9CVR6, Q9CVU6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program