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O00444

- PLK4_HUMAN

UniProt

O00444 - PLK4_HUMAN

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Protein
Serine/threonine-protein kinase PLK4
Gene
PLK4, SAK, STK18
Organism
Homo sapiens (Human)
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. 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. Phosphorylates CDC25C and CHEK2.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411ATP Inferred
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. protein binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. protein tyrosine kinase activity Source: InterPro

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: Reactome
  2. centriole replication Source: UniProtKB
  3. de novo centriole assembly Source: UniProtKB
  4. mitotic cell cycle Source: Reactome
  5. positive regulation of centriole replication Source: UniProtKB
  6. protein phosphorylation Source: ProtInc
  7. 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. 2681.
ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
SignaLinkiO00444.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:11397. PLK4.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Nucleusnucleolus By similarity. Cleavage furrow
Note: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Associates with centrioles throughout the cell cycle. According to 1 Publication, it is not present at cleavage furrows.2 Publications

GO - Cellular componenti

  1. centriole Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. cleavage furrow Source: UniProtKB-SubCell
  4. cytosol Source: Reactome
  5. deuterosome Source: UniProtKB
  6. nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411K → M: Abolishes ability to phosphorylate CDC25C and CHEK2. 2 Publications
Mutagenesisi154 – 1541D → A: Catalytically inactive mutant that causes some centrosome amplification above background levels when overexpressed. 1 Publication
Mutagenesisi170 – 1701T → D: Activating mutant. 2 Publications

Organism-specific databases

PharmGKBiPA36205.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 970970Serine/threonine-protein kinase PLK4
PRO_0000086567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei401 – 4011Phosphoserine2 Publications
Modified residuei817 – 8171Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO00444.
PRIDEiO00444.

PTM databases

PhosphoSiteiO00444.

Expressioni

Inductioni

Down-regulated in HCT 116 colorectal cancer cells, leading to aberrant centrioles composed of disorganized cylindrical microtubules and displaced appendages. Down-regulated by p53/TP53.2 Publications

Gene expression databases

ArrayExpressiO00444.
BgeeiO00444.
CleanExiHS_PLK4.
GenevestigatoriO00444.

Organism-specific databases

HPAiHPA035026.
HPA043198.

Interactioni

Subunit structurei

Homodimer By similarity. Interacts with CEP152 (via N-terminus).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SFNP319472EBI-746202,EBI-476295

Protein-protein interaction databases

BioGridi115956. 15 interactions.
DIPiDIP-34467N.
IntActiO00444. 6 interactions.
MINTiMINT-1460432.
STRINGi9606.ENSP00000270861.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 54
Helixi9 – 113
Beta strandi12 – 209
Beta strandi22 – 3110
Turni32 – 343
Beta strandi37 – 448
Helixi45 – 506
Helixi54 – 6411
Beta strandi75 – 806
Beta strandi82 – 909
Helixi97 – 1026
Beta strandi104 – 1063
Helixi110 – 12920
Helixi139 – 1413
Beta strandi142 – 1443
Beta strandi150 – 1523
Turni158 – 1614
Helixi193 – 20614
Helixi217 – 2259
Helixi236 – 24510
Helixi250 – 2523
Helixi256 – 2594
Turni263 – 2653

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3COKX-ray2.25A/B2-275[»]
4JXFX-ray2.40A4-269[»]
ProteinModelPortaliO00444.
SMRiO00444. Positions 4-319, 593-807, 890-964.

Miscellaneous databases

EvolutionaryTraceiO00444.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 265254Protein kinase
Add
BLAST
Domaini892 – 95665POLO box
Add
BLAST

Sequence similaritiesi

Contains 1 POLO box domain.

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG053617.
InParanoidiO00444.
KOiK08863.
OMAiMERCHSA.
OrthoDBiEOG7NCV33.
PhylomeDBiO00444.
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: O00444-1) [UniParc]FASTAAdd to Basket

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

MATCIGEKIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK    50
AGMVQRVQNE VKIHCQLKHP SILELYNYFE DSNYVYLVLE MCHNGEMNRY 100
LKNRVKPFSE NEARHFMHQI ITGMLYLHSH GILHRDLTLS NLLLTRNMNI 150
KIADFGLATQ LKMPHEKHYT LCGTPNYISP EIATRSAHGL ESDVWSLGCM 200
FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PSFLSIEAKD LIHQLLRRNP 250
ADRLSLSSVL DHPFMSRNSS TKSKDLGTVE DSIDSGHATI STAITASSST 300
SISGSLFDKR RLLIGQPLPN KMTVFPKNKS STDFSSSGDG NSFYTQWGNQ 350
ETSNSGRGRV IQDAEERPHS RYLRRAYSSD RSGTSNSQSQ AKTYTMERCH 400
SAEMLSVSKR SGGGENEERY SPTDNNANIF NFFKEKTSSS SGSFERPDNN 450
QALSNHLCPG KTPFPFADPT PQTETVQQWF GNLQINAHLR KTTEYDSISP 500
NRDFQGHPDL QKDTSKNAWT DTKVKKNSDA SDNAHSVKQQ NTMKYMTALH 550
SKPEIIQQEC VFGSDPLSEQ SKTRGMEPPW GYQNRTLRSI TSPLVAHRLK 600
PIRQKTKKAV VSILDSEEVC VELVKEYASQ EYVKEVLQIS SDGNTITIYY 650
PNGGRGFPLA DRPPSPTDNI SRYSFDNLPE KYWRKYQYAS RFVQLVRSKS 700
PKITYFTRYA KCILMENSPG ADFEVWFYDG VKIHKTEDFI QVIEKTGKSY 750
TLKSESEVNS LKEEIKMYMD HANEGHRICL ALESIISEEE RKTRSAPFFP 800
IIIGRKPGST SSPKALSPPP SVDSNYPTRE RASFNRMVMH SAASPTQAPI 850
LNPSMVTNEG LGLTTTASGT DISSNSLKDC LPKSAQLLKS VFVKNVGWAT 900
QLTSGAVWVQ FNDGSQLVVQ AGVSSISYTS PNGQTTRYGE NEKLPDYIKQ 950
KLQCLSSILL MFSNPTPNFH 970
Length:970
Mass (Da):108,972
Last modified:November 13, 2007 - v3
Checksum:i4D56F5FD983211A6
GO
Isoform 2 (identifier: O00444-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:938
Mass (Da):105,253
Checksum:i3605FA717C82C2B7
GO
Isoform 3 (identifier: O00444-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:929
Mass (Da):104,636
Checksum:iECD6808B29B9D8D9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti86 – 861Y → C.1 Publication
Corresponds to variant rs34156294 [ dbSNP | Ensembl ].
VAR_041027
Natural varianti146 – 1461R → H.1 Publication
Corresponds to variant rs35232579 [ dbSNP | Ensembl ].
VAR_041028
Natural varianti226 – 2261A → T.1 Publication
Corresponds to variant rs35448573 [ dbSNP | Ensembl ].
VAR_041029
Natural varianti232 – 2321S → T.4 Publications
Corresponds to variant rs3811740 [ dbSNP | Ensembl ].
VAR_019632
Natural varianti317 – 3171P → L.1 Publication
Corresponds to variant rs35049837 [ dbSNP | Ensembl ].
VAR_041030
Natural varianti449 – 4491N → D.1 Publication
Corresponds to variant rs34906574 [ dbSNP | Ensembl ].
VAR_041031
Natural varianti519 – 5191W → S.1 Publication
Corresponds to variant rs56043017 [ dbSNP | Ensembl ].
VAR_041032
Natural varianti830 – 8301E → D.4 Publications
Corresponds to variant rs17012739 [ dbSNP | Ensembl ].
VAR_041033

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4141Missing in isoform 3.
VSP_038116Add
BLAST
Alternative sequencei43 – 7432Missing in isoform 2.
VSP_038117Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341T → S in BAB69958. 1 Publication
Sequence conflicti58 – 581Q → K in CAA73575. 1 Publication
Sequence conflicti333 – 3331D → N in BAH13823. 1 Publication
Sequence conflicti387 – 3871S → R in BAB69958. 1 Publication
Sequence conflicti692 – 6921F → S in BAH13823. 1 Publication
Sequence conflicti696 – 6961V → L in BAB69958. 1 Publication
Sequence conflicti768 – 7681Y → F in CAA73575. 1 Publication
Sequence conflicti842 – 8421A → D in BAB69958. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3735.1. [O00444-1]
CCDS54803.1. [O00444-2]
CCDS54804.1. [O00444-3]
RefSeqiNP_001177728.1. NM_001190799.1. [O00444-2]
NP_001177730.1. NM_001190801.1. [O00444-3]
NP_055079.3. NM_014264.4. [O00444-1]
UniGeneiHs.172052.

Genome annotation databases

EnsembliENST00000270861; ENSP00000270861; ENSG00000142731. [O00444-1]
ENST00000513090; ENSP00000427554; ENSG00000142731. [O00444-2]
ENST00000514379; ENSP00000423582; ENSG00000142731. [O00444-3]
GeneIDi10733.
KEGGihsa:10733.
UCSCiuc003ifo.3. human. [O00444-1]
uc011cgs.2. human. [O00444-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3735.1. [O00444-1 ]
CCDS54803.1. [O00444-2 ]
CCDS54804.1. [O00444-3 ]
RefSeqi NP_001177728.1. NM_001190799.1. [O00444-2 ]
NP_001177730.1. NM_001190801.1. [O00444-3 ]
NP_055079.3. NM_014264.4. [O00444-1 ]
UniGenei Hs.172052.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3COK X-ray 2.25 A/B 2-275 [» ]
4JXF X-ray 2.40 A 4-269 [» ]
ProteinModelPortali O00444.
SMRi O00444. Positions 4-319, 593-807, 890-964.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115956. 15 interactions.
DIPi DIP-34467N.
IntActi O00444. 6 interactions.
MINTi MINT-1460432.
STRINGi 9606.ENSP00000270861.

Chemistry

BindingDBi O00444.
ChEMBLi CHEMBL3788.
GuidetoPHARMACOLOGYi 2171.

PTM databases

PhosphoSitei O00444.

Proteomic databases

PaxDbi O00444.
PRIDEi O00444.

Protocols and materials databases

DNASUi 10733.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000270861 ; ENSP00000270861 ; ENSG00000142731 . [O00444-1 ]
ENST00000513090 ; ENSP00000427554 ; ENSG00000142731 . [O00444-2 ]
ENST00000514379 ; ENSP00000423582 ; ENSG00000142731 . [O00444-3 ]
GeneIDi 10733.
KEGGi hsa:10733.
UCSCi uc003ifo.3. human. [O00444-1 ]
uc011cgs.2. human. [O00444-2 ]

Organism-specific databases

CTDi 10733.
GeneCardsi GC04P128802.
HGNCi HGNC:11397. PLK4.
HPAi HPA035026.
HPA043198.
MIMi 605031. gene.
neXtProti NX_O00444.
PharmGKBi PA36205.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG053617.
InParanoidi O00444.
KOi K08863.
OMAi MERCHSA.
OrthoDBi EOG7NCV33.
PhylomeDBi O00444.
TreeFami TF101090.

Enzyme and pathway databases

BRENDAi 2.7.11.21. 2681.
Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
SignaLinki O00444.

Miscellaneous databases

EvolutionaryTracei O00444.
GeneWikii PLK4.
GenomeRNAii 10733.
NextBioi 40744.
PROi O00444.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00444.
Bgeei O00444.
CleanExi HS_PLK4.
Genevestigatori O00444.

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. "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. 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. 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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. 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.

Entry informationi

Entry nameiPLK4_HUMAN
AccessioniPrimary (citable) accession number: O00444
Secondary accession number(s): B2RAL0
, B7Z837, B7Z8G7, Q8IYF0, Q96Q95, Q9UD84, Q9UDE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 13, 2007
Last modified: September 3, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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