O00444 (PLK4_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	970 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. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Ref.7 Ref.8 Ref.10 Ref.11 Ref.14 Ref.19
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Homodimer By similarity. Interacts with CEP152 (via N-terminus). Ref.17 Ref.18
Subcellular location	Cytoplasm › cytoskeleton › centrosome › centriole. Nucleus › nucleolus By similarity. Cleavage furrow. Note: Associates with centrioles throughout the cell cycle. According to Ref.8, it is not present at cleavage furrows. Ref.8 Ref.10
Induction	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. Ref.9 Ref.15
Post-translational modification	Ubiquitinated; leading to its degradation by the proteasome By similarity. Tyrosine-phosphorylated by TEC. Ref.2
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.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
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	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome centriole replication Inferred from mutant phenotype Ref.19. Source: UniProtKB positive regulation of centriole replication Inferred from mutant phenotype Ref.8Ref.10. Source: UniProtKB trophoblast giant cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	centriole Inferred from direct assay Ref.8Ref.10. Source: UniProtKB cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome nucleolus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.19. Source: UniProtKB protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SFN	P31947	2	EBI-746202,EBI-476295

Alternative products

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

Isoform 1 (identifier: O00444-1)

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: O00444-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: O00444-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 970

970

Serine/threonine-protein kinase PLK4

PRO_0000086567

Regions

Domain

12 – 265

254

Protein kinase

Domain

892 – 956

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 Probable

Amino acid modifications

Modified residue

401

1

Phosphoserine Ref.12 Ref.16

Modified residue

817

1

Phosphoserine Ref.16

Natural variations

Alternative sequence

1 – 41

41

Missing in isoform 3.

VSP_038116

Alternative sequence

43 – 74

32

Missing in isoform 2.

VSP_038117

Natural variant

86

1

Y → C. Ref.21
Corresponds to variant rs34156294 [ dbSNP | Ensembl ].

VAR_041027

Natural variant

146

1

R → H. Ref.21
Corresponds to variant rs35232579 [ dbSNP | Ensembl ].

VAR_041028

Natural variant

226

1

A → T. Ref.21
Corresponds to variant rs35448573 [ dbSNP | Ensembl ].

VAR_041029

Natural variant

232

1

S → T. Ref.1 Ref.2 Ref.3 Ref.21
Corresponds to variant rs3811740 [ dbSNP | Ensembl ].

VAR_019632

Natural variant

317

1

P → L. Ref.21
Corresponds to variant rs35049837 [ dbSNP | Ensembl ].

VAR_041030

Natural variant

449

1

N → D. Ref.21
Corresponds to variant rs34906574 [ dbSNP | Ensembl ].

VAR_041031

Natural variant

519

1

W → S. Ref.21
Corresponds to variant rs56043017 [ dbSNP | Ensembl ].

VAR_041032

Natural variant

830

1

E → D. Ref.1 Ref.2 Ref.3 Ref.21
Corresponds to variant rs17012739 [ dbSNP | Ensembl ].

VAR_041033

Experimental info

Mutagenesis

41

1

K → M: Abolishes ability to phosphorylate CDC25C and CHEK2. Ref.11 Ref.14

Mutagenesis

154

1

D → A: Catalytically inactive mutant that causes some centrosome amplification above background levels when overexpressed. Ref.8

Mutagenesis

170

1

T → D: Activating mutant. Ref.11 Ref.14

Sequence conflict

34

1

T → S in BAB69958. Ref.2

Sequence conflict

58

1

Q → K in CAA73575. Ref.1

Sequence conflict

333

1

D → N in BAH13823. Ref.3

Sequence conflict

387

1

S → R in BAB69958. Ref.2

Sequence conflict

692

1

F → S in BAH13823. Ref.3

Sequence conflict

696

1

V → L in BAB69958. Ref.2

Sequence conflict

768

1

Y → F in CAA73575. Ref.1

Sequence conflict

842

1

A → D in BAB69958. Ref.2

Secondary structure

1

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970

Helix Strand Turn

Details...

Helix

2 – 5

4

Helix

9 – 11

3

Beta strand

12 – 20

9

Beta strand

22 – 31

10

Turn

32 – 34

3

Beta strand

37 – 44

8

Helix

45 – 50

6

Helix

54 – 64

11

Beta strand

75 – 80

6

Beta strand

82 – 90

9

Helix

97 – 102

6

Helix

110 – 129

20

Helix

139 – 141

3

Beta strand

142 – 144

3

Beta strand

150 – 152

3

Helix

193 – 206

14

Helix

236 – 245

10

Helix

250 – 252

3

Helix

256 – 259

4

Turn

263 – 265

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 13, 2007. Version 3. Checksum: 4D56F5FD983211A6	FASTA	970	108,972
	10 20 30 40 50 60 MATCIGEKIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE 70 80 90 100 110 120 VKIHCQLKHP SILELYNYFE DSNYVYLVLE MCHNGEMNRY LKNRVKPFSE NEARHFMHQI 130 140 150 160 170 180 ITGMLYLHSH GILHRDLTLS NLLLTRNMNI KIADFGLATQ LKMPHEKHYT LCGTPNYISP 190 200 210 220 230 240 EIATRSAHGL ESDVWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PSFLSIEAKD 250 260 270 280 290 300 LIHQLLRRNP ADRLSLSSVL DHPFMSRNSS TKSKDLGTVE DSIDSGHATI STAITASSST 310 320 330 340 350 360 SISGSLFDKR RLLIGQPLPN KMTVFPKNKS STDFSSSGDG NSFYTQWGNQ ETSNSGRGRV 370 380 390 400 410 420 IQDAEERPHS RYLRRAYSSD RSGTSNSQSQ AKTYTMERCH SAEMLSVSKR SGGGENEERY 430 440 450 460 470 480 SPTDNNANIF NFFKEKTSSS SGSFERPDNN QALSNHLCPG KTPFPFADPT PQTETVQQWF 490 500 510 520 530 540 GNLQINAHLR KTTEYDSISP NRDFQGHPDL QKDTSKNAWT DTKVKKNSDA SDNAHSVKQQ 550 560 570 580 590 600 NTMKYMTALH SKPEIIQQEC VFGSDPLSEQ SKTRGMEPPW GYQNRTLRSI TSPLVAHRLK 610 620 630 640 650 660 PIRQKTKKAV VSILDSEEVC VELVKEYASQ EYVKEVLQIS SDGNTITIYY PNGGRGFPLA 670 680 690 700 710 720 DRPPSPTDNI SRYSFDNLPE KYWRKYQYAS RFVQLVRSKS PKITYFTRYA KCILMENSPG 730 740 750 760 770 780 ADFEVWFYDG VKIHKTEDFI QVIEKTGKSY TLKSESEVNS LKEEIKMYMD HANEGHRICL 790 800 810 820 830 840 ALESIISEEE RKTRSAPFFP IIIGRKPGST SSPKALSPPP SVDSNYPTRE RASFNRMVMH 850 860 870 880 890 900 SAASPTQAPI LNPSMVTNEG LGLTTTASGT DISSNSLKDC LPKSAQLLKS VFVKNVGWAT 910 920 930 940 950 960 QLTSGAVWVQ FNDGSQLVVQ AGVSSISYTS PNGQTTRYGE NEKLPDYIKQ KLQCLSSILL 970 MFSNPTPNFH
	Isoform 2 [UniParc]. Checksum: 3605FA717C82C2B7	FASTA	938	105,253
	10 20 30 40 50 60 MATCIGEKIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMLYNYFEDS NYVYLVLEMC 70 80 90 100 110 120 HNGEMNRYLK NRVKPFSENE ARHFMHQIIT GMLYLHSHGI LHRDLTLSNL LLTRNMNIKI 130 140 150 160 170 180 ADFGLATQLK MPHEKHYTLC GTPNYISPEI ATRSAHGLES DVWSLGCMFY TLLIGRPPFD 190 200 210 220 230 240 TDTVKNTLNK VVLADYEMPS FLSIEAKDLI HQLLRRNPAD RLSLSSVLDH PFMSRNSSTK 250 260 270 280 290 300 SKDLGTVEDS IDSGHATIST AITASSSTSI SGSLFDKRRL LIGQPLPNKM TVFPKNKSST 310 320 330 340 350 360 DFSSSGDGNS FYTQWGNQET SNSGRGRVIQ DAEERPHSRY LRRAYSSDRS GTSNSQSQAK 370 380 390 400 410 420 TYTMERCHSA EMLSVSKRSG GGENEERYSP TDNNANIFNF FKEKTSSSSG SFERPDNNQA 430 440 450 460 470 480 LSNHLCPGKT PFPFADPTPQ TETVQQWFGN LQINAHLRKT TEYDSISPNR DFQGHPDLQK 490 500 510 520 530 540 DTSKNAWTDT KVKKNSDASD NAHSVKQQNT MKYMTALHSK PEIIQQECVF GSDPLSEQSK 550 560 570 580 590 600 TRGMEPPWGY QNRTLRSITS PLVAHRLKPI RQKTKKAVVS ILDSEEVCVE LVKEYASQEY 610 620 630 640 650 660 VKEVLQISSD GNTITIYYPN GGRGFPLADR PPSPTDNISR YSFDNLPEKY WRKYQYASRF 670 680 690 700 710 720 VQLVRSKSPK ITYFTRYAKC ILMENSPGAD FEVWFYDGVK IHKTEDFIQV IEKTGKSYTL 730 740 750 760 770 780 KSESEVNSLK EEIKMYMDHA NEGHRICLAL ESIISEEERK TRSAPFFPII IGRKPGSTSS 790 800 810 820 830 840 PKALSPPPSV DSNYPTRERA SFNRMVMHSA ASPTQAPILN PSMVTNEGLG LTTTASGTDI 850 860 870 880 890 900 SSNSLKDCLP KSAQLLKSVF VKNVGWATQL TSGAVWVQFN DGSQLVVQAG VSSISYTSPN 910 920 930 GQTTRYGENE KLPDYIKQKL QCLSSILLMF SNPTPNFH
	Isoform 3 [UniParc]. Checksum: ECD6808B29B9D8D9	FASTA	929	104,636
	10 20 30 40 50 60 MIDKKAMYKA GMVQRVQNEV KIHCQLKHPS ILELYNYFED SNYVYLVLEM CHNGEMNRYL 70 80 90 100 110 120 KNRVKPFSEN EARHFMHQII TGMLYLHSHG ILHRDLTLSN LLLTRNMNIK IADFGLATQL 130 140 150 160 170 180 KMPHEKHYTL CGTPNYISPE IATRSAHGLE SDVWSLGCMF YTLLIGRPPF DTDTVKNTLN 190 200 210 220 230 240 KVVLADYEMP SFLSIEAKDL IHQLLRRNPA DRLSLSSVLD HPFMSRNSST KSKDLGTVED 250 260 270 280 290 300 SIDSGHATIS TAITASSSTS ISGSLFDKRR LLIGQPLPNK MTVFPKNKSS TDFSSSGDGN 310 320 330 340 350 360 SFYTQWGNQE TSNSGRGRVI QDAEERPHSR YLRRAYSSDR SGTSNSQSQA KTYTMERCHS 370 380 390 400 410 420 AEMLSVSKRS GGGENEERYS PTDNNANIFN FFKEKTSSSS GSFERPDNNQ ALSNHLCPGK 430 440 450 460 470 480 TPFPFADPTP QTETVQQWFG NLQINAHLRK TTEYDSISPN RDFQGHPDLQ KDTSKNAWTD 490 500 510 520 530 540 TKVKKNSDAS DNAHSVKQQN TMKYMTALHS KPEIIQQECV FGSDPLSEQS KTRGMEPPWG 550 560 570 580 590 600 YQNRTLRSIT SPLVAHRLKP IRQKTKKAVV SILDSEEVCV ELVKEYASQE YVKEVLQISS 610 620 630 640 650 660 DGNTITIYYP NGGRGFPLAD RPPSPTDNIS RYSFDNLPEK YWRKYQYASR FVQLVRSKSP 670 680 690 700 710 720 KITYFTRYAK CILMENSPGA DFEVWFYDGV KIHKTEDFIQ VIEKTGKSYT LKSESEVNSL 730 740 750 760 770 780 KEEIKMYMDH ANEGHRICLA LESIISEEER KTRSAPFFPI IIGRKPGSTS SPKALSPPPS 790 800 810 820 830 840 VDSNYPTRER ASFNRMVMHS AASPTQAPIL NPSMVTNEGL GLTTTASGTD ISSNSLKDCL 850 860 870 880 890 900 PKSAQLLKSV FVKNVGWATQ LTSGAVWVQF NDGSQLVVQA GVSSISYTSP NGQTTRYGEN 910 920 EKLPDYIKQK LQCLSSILLM FSNPTPNFH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Sak serine-threonine kinase acts as an effector of Tec tyrosine kinase." Yamashita Y., Kajigaya S., Yoshida K., Ueno S., Ota J., Ohmine K., Ueda M., Miyazato A., Ohya K., Kitamura T., Ozawa K., Mano H. J. Biol. Chem. 276:39012-39020(2001) [PubMed] [Europe PMC] [Abstract] 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]	"SAK/PLK4 is required for centriole duplication and flagella development." Bettencourt-Dias M., Rodrigues-Martins A., Carpenter L., Riparbelli M., Lehmann L., Gatt M.K., Carmo N., Balloux F., Callaini G., Glover D.M. Curr. Biol. 15:2199-2207(2005) [PubMed] [Europe PMC] [Abstract] 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]	"Plk4-induced centriole biogenesis in human cells." Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R., Stierhof Y.-D., Nigg E.A. Dev. Cell 13:190-202(2007) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-817, MASS SPECTROMETRY.
[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]	"Asterless is a scaffold for the onset of centriole assembly." Dzhindzhev N.S., Yu Q.D., Weiskopf K., Tzolovsky G., Cunha-Ferreira I., Riparbelli M., Rodrigues-Martins A., Bettencourt-Dias M., Callaini G., Glover D.M. Nature 467:714-718(2010) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00410344.
IPI00944477.
IPI00944493.

RefSeq

NP_001177728.1. NM_001190799.1.
NP_001177730.1. NM_001190801.1.
NP_055079.3. NM_014264.4.

UniGene

Hs.172052.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3COK	X-ray	2.25	A/B	2-275	[»]

ProteinModelPortal

O00444.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34467N.

IntAct

O00444. 4 interactions.

MINT

MINT-1460432.

STRING

9606.ENSP00000270861.

PTM databases

PhosphoSite

O00444.

Proteomic databases

PaxDb

O00444.

PRIDE

O00444.

Protocols and materials databases

DNASU

10733.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000270861; ENSP00000270861; ENSG00000142731.
ENST00000513090; ENSP00000427554; ENSG00000142731.
ENST00000514379; ENSP00000423582; ENSG00000142731.

GeneID

10733.

KEGG

hsa:10733.

UCSC

uc003ifo.3. human.
uc011cgs.2. human.

Organism-specific databases

CTD

10733.

GeneCards

GC04P128802.

HGNC

HGNC:11397. PLK4.

HPA

HPA035026.

MIM

605031. gene.

neXtProt

NX_O00444.

PharmGKB

PA36205.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG053617.

InParanoid

O00444.

KO

K08863.

OMA

APFFPII.

OrthoDB

EOG4W9J37.

PhylomeDB

O00444.

Enzyme and pathway databases

BRENDA

2.7.11.21. 2681.

Reactome

REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpress

O00444.

Bgee

O00444.

CleanEx

HS_PLK4.

Genevestigator

O00444.

GermOnline

ENSG00000142731. Homo sapiens.

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

BindingDB

O00444.

ChEMBL

CHEMBL3788.

EvolutionaryTrace

O00444.

GenomeRNAi

10733.

NextBio

40744.

SOURCE

Search...

Entry information

Entry name

PLK4_HUMAN

Accession

Primary (citable) accession number: O00444
Secondary accession number(s): B2RAL0 , B7Z837, B7Z8G7, Q8IYF0, Q96Q95, Q9UD84, Q9UDE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	November 13, 2007
Last modified:	May 1, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.