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Protein

Serine/threonine-protein kinase PLK3

Gene

PLK3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1.25 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911ATPPROSITE-ProRule annotation
Active sitei185 – 1851Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi68 – 769ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • p53 binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cytoplasmic microtubule organization Source: UniProtKB
  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  • endomitotic cell cycle Source: UniProtKB
  • G1/S transition of mitotic cell cycle Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • Golgi disassembly Source: UniProtKB
  • mitotic cell cycle checkpoint Source: UniProtKB
  • mitotic G1/S transition checkpoint Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of intracellular protein transport Source: UniProtKB
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia Source: UniProtKB
  • protein kinase B signaling Source: UniProtKB
  • protein phosphorylation Source: ProtInc
  • regulation of cell division Source: UniProtKB
  • regulation of cytokinesis Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • response to osmotic stress Source: UniProtKB
  • response to radiation Source: UniProtKB
  • response to reactive oxygen species Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.21. 2681.
ReactomeiR-HSA-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
SignaLinkiQ9H4B4.
SIGNORiQ9H4B4.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PLK3 (EC:2.7.11.21)
Alternative name(s):
Cytokine-inducible serine/threonine-protein kinase
FGF-inducible kinase
Polo-like kinase 3
Short name:
PLK-3
Proliferation-related kinase
Gene namesi
Name:PLK3
Synonyms:CNK, FNK, PRK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2154. PLK3.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • dendrite Source: Ensembl
  • Golgi stack Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi91 – 911K → R: Kinase defective mutant, abolishes activity. 7 Publications
Mutagenesisi203 – 2031D → A: Kinase defective mutant, abolishes activity. 1 Publication
Mutagenesisi219 – 2191T → E: Kinase-defective mutant. 1 Publication
Mutagenesisi467 – 4682WV → FA: Abolishes localization to the centrosome and ability to induce the G2/M arrest. 1 Publication

Organism-specific databases

PharmGKBiPA26664.

Chemistry

ChEMBLiCHEMBL4897.
GuidetoPHARMACOLOGYi2170.

Polymorphism and mutation databases

BioMutaiPLK3.
DMDMi51338822.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 646646Serine/threonine-protein kinase PLK3PRO_0000086564Add
BLAST

Post-translational modificationi

Phosphorylated in an ATM-dependent manner following DNA damage. Phosphorylated as cells enter mitosis and dephosphorylated as cells exit mitosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9H4B4.
PRIDEiQ9H4B4.

PTM databases

iPTMnetiQ9H4B4.
PhosphoSiteiQ9H4B4.

Expressioni

Tissue specificityi

Transcripts are highly detected in placenta, lung, followed by skeletal muscle, heart, pancreas, ovaries and kidney and weakly detected in liver and brain. May have a short half-live. In cells of hematopoietic origin, strongly and exclusively detected in terminally differentiated macrophages. Transcript expression appears to be down-regulated in primary lung tumor.

Developmental stagei

Expression is cell cycle regulated with a peak in G1 phase.1 Publication

Inductioni

Cytokine and cellular adhesion trigger induction. Down-regulated in a majority of lung carcinoma samples.1 Publication

Gene expression databases

BgeeiQ9H4B4.
CleanExiHS_PLK3.
GenevisibleiQ9H4B4. HS.

Organism-specific databases

HPAiHPA060318.

Interactioni

Subunit structurei

Interacts (via the POLO-box domain) with CIB1; leading to inhibit PLK3 kinase activity. Interacts with GOLGB1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
POU2F1P148593EBI-751877,EBI-624770
PRNPP041564EBI-751877,EBI-977302
VRK1Q9998612EBI-751877,EBI-1769146

GO - Molecular functioni

  • p53 binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107663. 13 interactions.
IntActiQ9H4B4. 4 interactions.
MINTiMINT-110679.
STRINGi9606.ENSP00000361275.

Chemistry

BindingDBiQ9H4B4.

Structurei

Secondary structure

1
646
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi62 – 698Combined sources
Beta strandi75 – 817Combined sources
Turni82 – 843Combined sources
Beta strandi87 – 948Combined sources
Helixi95 – 984Combined sources
Helixi101 – 11414Combined sources
Beta strandi125 – 1306Combined sources
Beta strandi132 – 1398Combined sources
Helixi147 – 1548Combined sources
Helixi159 – 17820Combined sources
Helixi188 – 1903Combined sources
Beta strandi191 – 1933Combined sources
Beta strandi199 – 2013Combined sources
Turni213 – 2153Combined sources
Turni224 – 2263Combined sources
Helixi229 – 2324Combined sources
Helixi239 – 25517Combined sources
Helixi265 – 2739Combined sources
Helixi285 – 29410Combined sources
Helixi299 – 3013Combined sources
Helixi305 – 3095Combined sources
Helixi312 – 3154Combined sources
Helixi325 – 3284Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B6LX-ray1.90A52-332[»]
ProteinModelPortaliQ9H4B4.
SMRiQ9H4B4. Positions 52-332, 429-640.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 314253Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini470 – 53768POLO box 1PROSITE-ProRule annotationAdd
BLAST
Domaini567 – 63771POLO box 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK3 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them (By similarity). The POLO box domains mediates localization to the centrosome.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.PROSITE-ProRule annotation
Contains 2 POLO box domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0575. Eukaryota.
ENOG410XQBP. LUCA.
GeneTreeiENSGT00530000062954.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiQ9H4B4.
KOiK08862.
OMAiLCALRNC.
OrthoDBiEOG78M01K.
PhylomeDBiQ9H4B4.
TreeFamiTF101089.

Family and domain databases

Gene3Di3.30.1120.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
IPR000959. POLO_box_duplicated_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR020658. Ser/Thr_kinase_Plk3.
[Graphical view]
PANTHERiPTHR24345:SF42. PTHR24345:SF42. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H4B4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPAAGFLSP RPFQRAAAAP APPAGPGPPP SALRGPELEM LAGLPTSDPG
60 70 80 90 100
RLITDPRSGR TYLKGRLLGK GGFARCYEAT DTETGSAYAV KVIPQSRVAK
110 120 130 140 150
PHQREKILNE IELHRDLQHR HIVRFSHHFE DADNIYIFLE LCSRKSLAHI
160 170 180 190 200
WKARHTLLEP EVRYYLRQIL SGLKYLHQRG ILHRDLKLGN FFITENMELK
210 220 230 240 250
VGDFGLAARL EPPEQRKKTI CGTPNYVAPE VLLRQGHGPE ADVWSLGCVM
260 270 280 290 300
YTLLCGSPPF ETADLKETYR CIKQVHYTLP ASLSLPARQL LAAILRASPR
310 320 330 340 350
DRPSIDQILR HDFFTKGYTP DRLPISSCVT VPDLTPPNPA RSLFAKVTKS
360 370 380 390 400
LFGRKKKSKN HAQERDEVSG LVSGLMRTSV GHQDARPEAP AASGPAPVSL
410 420 430 440 450
VETAPEDSSP RGTLASSGDG FEEGLTVATV VESALCALRN CIAFMPPAEQ
460 470 480 490 500
NPAPLAQPEP LVWVSKWVDY SNKFGFGYQL SSRRVAVLFN DGTHMALSAN
510 520 530 540 550
RKTVHYNPTS TKHFSFSVGA VPRALQPQLG ILRYFASYME QHLMKGGDLP
560 570 580 590 600
SVEEVEVPAP PLLLQWVKTD QALLMLFSDG TVQVNFYGDH TKLILSGWEP
610 620 630 640
LLVTFVARNR SACTYLASHL RQLGCSPDLR QRLRYALRLL RDRSPA
Length:646
Mass (Da):71,629
Last modified:August 16, 2004 - v2
Checksum:i324CA3E9DE482514
GO

Sequence cautioni

The sequence AAC50637.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161A → T in CAC10659 (PubMed:11039900).Curated
Sequence conflicti20 – 201P → T in CAC10659 (PubMed:11039900).Curated
Sequence conflicti99 – 991A → V in CAC10659 (PubMed:11039900).Curated
Sequence conflicti353 – 3531G → V in CAC10659 (PubMed:11039900).Curated
Sequence conflicti419 – 4191D → H in CAC10659 (PubMed:11039900).Curated
Sequence conflicti464 – 4707VSKWVDY → FSEWVGF in CAC10659 (PubMed:11039900).Curated
Sequence conflicti522 – 5221P → R in CAC10659 (PubMed:11039900).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611T → S.1 Publication
Corresponds to variant rs17884581 [ dbSNP | Ensembl ].
VAR_021091
Natural varianti68 – 681L → F.1 Publication
Corresponds to variant rs17884316 [ dbSNP | Ensembl ].
VAR_021092
Natural varianti283 – 2831L → F.1 Publication
Corresponds to variant rs17880471 [ dbSNP | Ensembl ].
VAR_021093
Natural varianti483 – 4831R → C.1 Publication
Corresponds to variant rs17884653 [ dbSNP | Ensembl ].
VAR_021094
Natural varianti491 – 4911D → N.1 Publication
Corresponds to variant rs17855444 [ dbSNP | Ensembl ].
VAR_062384
Natural varianti498 – 4981S → L.1 Publication
Corresponds to variant rs17880829 [ dbSNP | Ensembl ].
VAR_021095
Natural varianti618 – 6181S → P.1 Publication
Corresponds to variant rs17881786 [ dbSNP | Ensembl ].
VAR_021096

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293866 mRNA. Translation: CAC10659.1.
AY764184 Genomic DNA. Translation: AAU88146.1.
AL592166 Genomic DNA. Translation: CAI13006.1.
CH471059 Genomic DNA. Translation: EAX07021.1.
BC013899 mRNA. Translation: AAH13899.1.
U56998 mRNA. Translation: AAC50637.1. Different initiation.
CCDSiCCDS515.1.
RefSeqiNP_004064.2. NM_004073.3.
UniGeneiHs.632415.

Genome annotation databases

EnsembliENST00000372201; ENSP00000361275; ENSG00000173846.
GeneIDi1263.
KEGGihsa:1263.
UCSCiuc001cmn.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293866 mRNA. Translation: CAC10659.1.
AY764184 Genomic DNA. Translation: AAU88146.1.
AL592166 Genomic DNA. Translation: CAI13006.1.
CH471059 Genomic DNA. Translation: EAX07021.1.
BC013899 mRNA. Translation: AAH13899.1.
U56998 mRNA. Translation: AAC50637.1. Different initiation.
CCDSiCCDS515.1.
RefSeqiNP_004064.2. NM_004073.3.
UniGeneiHs.632415.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B6LX-ray1.90A52-332[»]
ProteinModelPortaliQ9H4B4.
SMRiQ9H4B4. Positions 52-332, 429-640.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107663. 13 interactions.
IntActiQ9H4B4. 4 interactions.
MINTiMINT-110679.
STRINGi9606.ENSP00000361275.

Chemistry

BindingDBiQ9H4B4.
ChEMBLiCHEMBL4897.
GuidetoPHARMACOLOGYi2170.

PTM databases

iPTMnetiQ9H4B4.
PhosphoSiteiQ9H4B4.

Polymorphism and mutation databases

BioMutaiPLK3.
DMDMi51338822.

Proteomic databases

PaxDbiQ9H4B4.
PRIDEiQ9H4B4.

Protocols and materials databases

DNASUi1263.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372201; ENSP00000361275; ENSG00000173846.
GeneIDi1263.
KEGGihsa:1263.
UCSCiuc001cmn.4. human.

Organism-specific databases

CTDi1263.
GeneCardsiPLK3.
H-InvDBHIX0199969.
HGNCiHGNC:2154. PLK3.
HPAiHPA060318.
MIMi602913. gene.
neXtProtiNX_Q9H4B4.
PharmGKBiPA26664.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0575. Eukaryota.
ENOG410XQBP. LUCA.
GeneTreeiENSGT00530000062954.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiQ9H4B4.
KOiK08862.
OMAiLCALRNC.
OrthoDBiEOG78M01K.
PhylomeDBiQ9H4B4.
TreeFamiTF101089.

Enzyme and pathway databases

BRENDAi2.7.11.21. 2681.
ReactomeiR-HSA-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
SignaLinkiQ9H4B4.
SIGNORiQ9H4B4.

Miscellaneous databases

ChiTaRSiPLK3. human.
GeneWikiiPLK3.
GenomeRNAii1263.
PROiQ9H4B4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H4B4.
CleanExiHS_PLK3.
GenevisibleiQ9H4B4. HS.

Family and domain databases

Gene3Di3.30.1120.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
IPR000959. POLO_box_duplicated_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR020658. Ser/Thr_kinase_Plk3.
[Graphical view]
PANTHERiPTHR24345:SF42. PTHR24345:SF42. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Adhesion induced expression of the serine/threonine kinase Fnk in human macrophages."
    Holtrich U., Wolf G., Yuan J., Bereiter-Hahn J., Karn T., Weiler M., Kauselmann G., Rehli M., Andreesen R., Kaufmann M., Kuhl D., Strebhardt K.
    Oncogene 19:4832-4839(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  2. NIEHS SNPs program
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-61; PHE-68; PHE-283; CYS-483; LEU-498 AND PRO-618.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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], VARIANT ASN-491.
    Tissue: Brain.
  6. "Prk, a cytokine-inducible human protein serine/threonine kinase whose expression appears to be down-regulated in lung carcinomas."
    Li B., Ouyang B., Pan H., Reissmann P.T., Slamon D.J., Arceci R., Lu L., Dai W.
    J. Biol. Chem. 271:19402-19408(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-646.
    Tissue: Placenta.
  7. "Intron/exon organization and polymorphisms of the PLK3/PRK gene in human lung carcinoma cell lines."
    Wiest J., Clark A.M., Dai W.
    Genes Chromosomes Cancer 32:384-389(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Mammalian Polo-like kinase 3 (Plk3) is a multifunctional protein involved in stress response pathways."
    Bahassi el M., Conn C.W., Myer D.L., Hennigan R.F., McGowan C.H., Sanchez Y., Stambrook P.J.
    Oncogene 21:6633-6640(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TP53 AND CHEK2, PHOSPHORYLATION.
  9. "Human Prk is a conserved protein serine/threonine kinase involved in regulating M phase functions."
    Ouyang B., Pan H., Lu L., Li J., Stambrook P., Li B., Dai W.
    J. Biol. Chem. 272:28646-28651(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The physical association and phosphorylation of Cdc25C protein phosphatase by Prk."
    Ouyang B., Li W., Pan H., Meadows J., Hoffmann I., Dai W.
    Oncogene 18:6029-6036(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Incomplete cytokinesis and induction of apoptosis by overexpression of the mammalian polo-like kinase, Plk3."
    Conn C.W., Hennigan R.F., Dai W., Sanchez Y., Stambrook P.J.
    Cancer Res. 60:6826-6831(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-203.
  12. "Reactive oxygen species-induced phosphorylation of p53 on serine 20 is mediated in part by polo-like kinase-3."
    Xie S., Wang Q., Wu H., Cogswell J., Lu L., Jhanwar-Uniyal M., Dai W.
    J. Biol. Chem. 276:36194-36199(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TP53, MUTAGENESIS OF LYS-91.
  13. "Plk3 functionally links DNA damage to cell cycle arrest and apoptosis at least in part via the p53 pathway."
    Xie S., Wu H., Wang Q., Cogswell J.P., Husain I., Conn C., Stambrook P., Jhanwar-Uniyal M., Dai W.
    J. Biol. Chem. 276:43305-43312(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TP53.
  14. "Cell cycle arrest and apoptosis induced by human Polo-like kinase 3 is mediated through perturbation of microtubule integrity."
    Wang Q., Xie S., Chen J., Fukasawa K., Naik U., Traganos F., Darzynkiewicz Z., Jhanwar-Uniyal M., Dai W.
    Mol. Cell. Biol. 22:3450-3459(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Polo-like kinase 3 is Golgi localized and involved in regulating Golgi fragmentation during the cell cycle."
    Ruan Q., Wang Q., Xie S., Fang Y., Darzynkiewicz Z., Guan K., Jhanwar-Uniyal M., Dai W.
    Exp. Cell Res. 294:51-59(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GOLGB1, MUTAGENESIS OF LYS-91.
  16. "Cdc25C phosphorylation on serine 191 by Plk3 promotes its nuclear translocation."
    Bahassi el M., Hennigan R.F., Myer D.L., Stambrook P.J.
    Oncogene 23:2658-2663(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CDC25C.
  17. "MEK1-induced Golgi dynamics during cell cycle progression is partly mediated by Polo-like kinase-3."
    Xie S., Wang Q., Ruan Q., Liu T., Jhanwar-Uniyal M., Guan K., Dai W.
    Oncogene 23:3822-3829(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Polo box domain of Plk3 functions as a centrosome localization signal, overexpression of which causes mitotic arrest, cytokinesis defects, and apoptosis."
    Jiang N., Wang X., Jhanwar-Uniyal M., Darzynkiewicz Z., Dai W.
    J. Biol. Chem. 281:10577-10582(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-219 AND 467-TRP-VAL-468.
  19. "Priming phosphorylation of Chk2 by polo-like kinase 3 (Plk3) mediates its full activation by ATM and a downstream checkpoint in response to DNA damage."
    Bahassi el M., Myer D.L., McKenney R.J., Hennigan R.F., Stambrook P.J.
    Mutat. Res. 596:166-176(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TP53 AND CHEK2.
  20. "Stress-induced c-Jun activation mediated by Polo-like kinase 3 in corneal epithelial cells."
    Wang L., Dai W., Lu L.
    J. Biol. Chem. 282:32121-32127(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF JUN, MUTAGENESIS OF LYS-91.
  21. "Polo-like kinase 3 is required for entry into S phase."
    Zimmerman W.C., Erikson R.L.
    Proc. Natl. Acad. Sci. U.S.A. 104:1847-1852(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  22. "Plk3 phosphorylates topoisomerase IIalpha at Thr(1342), a site that is not recognized by Plk1."
    Iida M., Matsuda M., Komatani H.
    Biochem. J. 411:27-32(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TOP2A.
  23. "Activation of Polo-like kinase 3 by hypoxic stresses."
    Wang L., Gao J., Dai W., Lu L.
    J. Biol. Chem. 283:25928-25935(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF JUN, SUBCELLULAR LOCATION.
  24. "Plk3 inhibits pro-apoptotic activity of p73 through physical interaction and phosphorylation."
    Sang M., Ando K., Okoshi R., Koida N., Li Y., Zhu Y., Shimozato O., Geng C., Shan B., Nakagawara A., Ozaki T.
    Genes Cells 14:775-788(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TP73, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-91.
  25. "Plk3 interacts with and specifically phosphorylates VRK1 in Ser342, a downstream target in a pathway that induces Golgi fragmentation."
    Lopez-Sanchez I., Sanz-Garcia M., Lazo P.A.
    Mol. Cell. Biol. 29:1189-1201(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF VRK1, MUTAGENESIS OF LYS-91.
  26. "Plk3 functions as an essential component of the hypoxia regulatory pathway by direct phosphorylation of HIF-1alpha."
    Xu D., Yao Y., Lu L., Costa M., Dai W.
    J. Biol. Chem. 285:38944-38950(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HIF1A, MUTAGENESIS OF LYS-91.
  27. "Regulation of PTEN stability and activity by Plk3."
    Xu D., Yao Y., Jiang X., Lu L., Dai W.
    J. Biol. Chem. 285:39935-39942(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PTEN, MUTAGENESIS OF LYS-91.
  28. "Calcium- and integrin-binding protein 1 regulates microtubule organization and centrosome segregation through polo like kinase 3 during cell cycle progression."
    Naik M.U., Naik U.P.
    Int. J. Biochem. Cell Biol. 43:120-129(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CIB1, SUBCELLULAR LOCATION.
  29. "Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1 in breast cancer cells."
    Naik M.U., Pham N.T., Beebe K., Dai W., Naik U.P.
    Int. J. Cancer 128:587-596(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIB1.
  30. "Hyperosmotic stress-induced ATF-2 activation through Polo-like kinase 3 in human corneal epithelial cells."
    Wang L., Payton R., Dai W., Lu L.
    J. Biol. Chem. 286:1951-1958(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ATF2, SUBCELLULAR LOCATION.
  31. "Bcl-xL phosphorylation at Ser49 by polo kinase 3 during cell cycle progression and checkpoints."
    Wang J., Beauchemin M., Bertrand R.
    Cell. Signal. 23:2030-2038(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BCL2L1.
  32. "Absence of polo-like kinase 3 in mice stabilizes Cdc25A after DNA damage but is not sufficient to produce tumors."
    Myer D.L., Robbins S.B., Yin M., Boivin G.P., Liu Y., Greis K.D., Bahassi el M., Stambrook P.J.
    Mutat. Res. 714:1-10(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CDC25A.
  33. "Calcium- and integrin-binding protein 1 regulates endomitosis and its interaction with Polo-like kinase 3 is enhanced in endomitotic Dami cells."
    Kostyak J.C., Naik U.P.
    PLoS ONE 6:E14513-E14513(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CIB1.
  34. "Multifaceted polo-like kinases: drug targets and antitargets for cancer therapy."
    Strebhardt K.
    Nat. Rev. Drug Discov. 9:643-660(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.

Entry informationi

Entry nameiPLK3_HUMAN
AccessioniPrimary (citable) accession number: Q9H4B4
Secondary accession number(s): Q15767, Q5JR99, Q96CV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: August 16, 2004
Last modified: June 8, 2016
This is version 153 of the entry and version 2 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 1
    Human chromosome 1: 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

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 one 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.