Q9H4B4 (PLK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PLK3
Synonyms:	CNK, FNK, PRK

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	646 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31 Ref.32 Ref.33
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts (via the POLO-box domain) with CIB1; leading to ihnibit PLK3 kinase activity. Interacts with GOLGB1. Ref.15 Ref.29 Ref.33
Subcellular location	Cytoplasm. Nucleus. Nucleus › nucleolus. Golgi apparatus. Cytoplasm › cytoskeleton › centrosome. Note: Translocates to the nucleus upon cisplatin treatment. Localizes to the Golgi apparatus during interphase. According to a report, PLK3 localizes only in the nucleolus and not in the centrosome, or in any other location in the cytoplasm (Ref.21). The discrepancies in results may be explained by the PLK3 antibody specificity, by cell line-specific expression or post-translational modifications. Ref.15 Ref.18 Ref.21 Ref.23 Ref.25 Ref.30
Tissue specificity	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 stage	Expression is cell cycle regulated with a peak in G1 phase. Ref.21
Induction	Cytokine and cellular adhesion trigger induction. Down-regulated in a majority of lung carcinoma samples. Ref.7
Domain	The POLO box domains act as phosphopeptide-binding module that recongnize 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.
Post-translational modification	Phosphorylated in an ATM-dependent manner following DNA damage. Phosphorylated as cells enter mitosis and dephosphorylated as cells exit mitosis. Ref.8 Ref.12 Ref.13 Ref.16 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31 Ref.32
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily. Contains 2 POLO box domains. Contains 1 protein kinase domain.
Sequence caution	The sequence AAC50637.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle DNA damage
Cellular component	Cytoplasm Cytoskeleton Golgi apparatus Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	G1/S transition checkpoint Inferred from sequence or structural similarity. Source: UniProtKB G1/S transition of mitotic cell cycle Inferred from mutant phenotype Ref.21. Source: UniProtKB Golgi disassembly Inferred from direct assay Ref.15Ref.26. Source: UniProtKB S phase of mitotic cell cycle Inferred from mutant phenotype Ref.21. Source: UniProtKB apoptotic process Traceable author statement Ref.18. Source: UniProtKB cytokinesis Traceable author statement Ref.18Ref.31. Source: UniProtKB endomitotic cell cycle Traceable author statement Ref.33. Source: UniProtKB mitotic cell cycle G2/M transition checkpoint Traceable author statement Ref.31. Source: UniProtKB negative regulation of apoptotic process Inferred from direct assay Ref.25. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.25. Source: UniProtKB positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia Inferred from direct assay Ref.27. Source: UniProtKB protein kinase B signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB response to DNA damage stimulus Inferred from direct assay Ref.25. Source: UniProtKB response to osmotic stress Inferred from direct assay Ref.30. Source: UniProtKB response to radiation Inferred from direct assay Ref.32. Source: UniProtKB response to reactive oxygen species Inferred from direct assay Ref.12. Source: UniProtKB
Cellular component	Golgi stack Inferred from direct assay Ref.15. Source: UniProtKB centrosome Inferred from direct assay Ref.18. Source: UniProtKB membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay Ref.21. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW p53 binding Inferred from direct assay Ref.12. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.12Ref.16Ref.19Ref.26Ref.27Ref.30Ref.32Ref.31. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRNP	P04156	4	EBI-751877,EBI-977302
VRK1	Q99986	12	EBI-751877,EBI-1769146

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 646	646	Serine/threonine-protein kinase PLK3		PRO_0000086564
Regions
	Domain	62 – 314	253	Protein kinase
	Domain	470 – 537	68	POLO box 1
	Domain	567 – 637	71	POLO box 2
	Nucleotide binding	68 – 76	9	ATP By similarity
Sites
	Active site	185	1	Proton acceptor By similarity
	Binding site	91	1	ATP By similarity
Amino acid modifications
	Modified residue	219	1	Phosphothreonine By similarity
	Modified residue	348	1	Phosphothreonine Ref.24
Natural variations
	Natural variant	61	1	T → S. Ref.2 Corresponds to variant rs17884581 [ dbSNP | Ensembl ].		VAR_021091
	Natural variant	68	1	L → F. Ref.2 Corresponds to variant rs17884316 [ dbSNP | Ensembl ].		VAR_021092
	Natural variant	283	1	L → F. Ref.2 Corresponds to variant rs17880471 [ dbSNP | Ensembl ].		VAR_021093
	Natural variant	483	1	R → C. Ref.2 Corresponds to variant rs17884653 [ dbSNP | Ensembl ].		VAR_021094
	Natural variant	491	1	D → N. Ref.5 Corresponds to variant rs17855444 [ dbSNP | Ensembl ].		VAR_062384
	Natural variant	498	1	S → L. Ref.2 Corresponds to variant rs17880829 [ dbSNP | Ensembl ].		VAR_021095
	Natural variant	618	1	S → P. Ref.2 Corresponds to variant rs17881786 [ dbSNP | Ensembl ].		VAR_021096
Experimental info
	Mutagenesis	91	1	K → R: Kinase defective mutant, abolishes activity. Ref.12 Ref.15 Ref.20 Ref.25 Ref.26 Ref.27 Ref.28
	Mutagenesis	203	1	D → A: Kinase defective mutant, abolishes activity. Ref.11
	Mutagenesis	219	1	T → E: Kinase-defective mutant. Ref.18
	Mutagenesis	467 – 468	2	WV → FA: Abolishes localization to the centrosome and ability to induce the G2/M arrest.
	Sequence conflict	16	1	A → T in CAC10659. Ref.1
	Sequence conflict	20	1	P → T in CAC10659. Ref.1
	Sequence conflict	99	1	A → V in CAC10659. Ref.1
	Sequence conflict	353	1	G → V in CAC10659. Ref.1
	Sequence conflict	419	1	D → H in CAC10659. Ref.1
	Sequence conflict	464 – 470	7	VSKWVDY → FSEWVGF in CAC10659. Ref.1
	Sequence conflict	522	1	P → R in CAC10659. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9H4B4 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 324CA3E9DE482514	FASTA	646	71,629
	10 20 30 40 50 60 MEPAAGFLSP RPFQRAAAAP APPAGPGPPP SALRGPELEM LAGLPTSDPG RLITDPRSGR 70 80 90 100 110 120 TYLKGRLLGK GGFARCYEAT DTETGSAYAV KVIPQSRVAK PHQREKILNE IELHRDLQHR 130 140 150 160 170 180 HIVRFSHHFE DADNIYIFLE LCSRKSLAHI WKARHTLLEP EVRYYLRQIL SGLKYLHQRG 190 200 210 220 230 240 ILHRDLKLGN FFITENMELK VGDFGLAARL EPPEQRKKTI CGTPNYVAPE VLLRQGHGPE 250 260 270 280 290 300 ADVWSLGCVM YTLLCGSPPF ETADLKETYR CIKQVHYTLP ASLSLPARQL LAAILRASPR 310 320 330 340 350 360 DRPSIDQILR HDFFTKGYTP DRLPISSCVT VPDLTPPNPA RSLFAKVTKS LFGRKKKSKN 370 380 390 400 410 420 HAQERDEVSG LVSGLMRTSV GHQDARPEAP AASGPAPVSL VETAPEDSSP RGTLASSGDG 430 440 450 460 470 480 FEEGLTVATV VESALCALRN CIAFMPPAEQ NPAPLAQPEP LVWVSKWVDY SNKFGFGYQL 490 500 510 520 530 540 SSRRVAVLFN DGTHMALSAN RKTVHYNPTS TKHFSFSVGA VPRALQPQLG ILRYFASYME 550 560 570 580 590 600 QHLMKGGDLP SVEEVEVPAP PLLLQWVKTD QALLMLFSDG TVQVNFYGDH TKLILSGWEP 610 620 630 640 LLVTFVARNR SACTYLASHL RQLGCSPDLR QRLRYALRLL RDRSPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11039900] [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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 8702627] [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: 11746980] [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: 12242661] [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: 9353331] [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: 10557092] [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: 11156373] [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: 11447225] [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: 11551930] [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: 11971976] [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: 14980500] [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: 14968113] [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: 15021912] [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: 16478733] [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: 16481012] [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: 17804415] [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: 17264206] [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: 18062778] [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: 18650425] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF JUN, SUBCELLULAR LOCATION.
[24]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-348, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[25]	"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: 19490146] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TP73, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-91.
[26]	"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: 19103756] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF VRK1, MUTAGENESIS OF LYS-91.
[27]	"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: 20889502] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HIF1A, MUTAGENESIS OF LYS-91.
[28]	"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: 20940307] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PTEN, MUTAGENESIS OF LYS-91.
[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: 20473878] [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: 21098032] [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: 21840391] [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: 21376736] [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: 21264284] [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: 20671765] [Abstract] Cited for: REVIEW ON FUNCTION.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00304186.
RefSeq	NP_004064.2. NM_004073.2.
UniGene	Hs.632415.
3D structure databases
ProteinModelPortal	Q9H4B4.
SMR	Q9H4B4. Positions 48-335, 455-643.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H4B4. 3 interactions.
MINT	MINT-110679.
STRING	Q9H4B4.
Polymorphism databases
DMDM	51338822.
Proteomic databases
PRIDE	Q9H4B4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000372201; ENSP00000361275; ENSG00000173846.
GeneID	1263.
KEGG	hsa:1263.
UCSC	uc001cmn.1. human.
Organism-specific databases
CTD	1263.
GeneCards	GC01P045265.
H-InvDB	HIX0199969.
HGNC	HGNC:2154. PLK3.
MIM	602913. gene.
neXtProt	NX_Q9H4B4.
PharmGKB	PA26664.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10409.
GeneTree	ENSGT00530000062954.
HOGENOM	HBG738952.
HOVERGEN	HBG001843.
InParanoid	Q9H4B4.
OMA	PRSGRTY.
OrthoDB	EOG4GHZNR.
PhylomeDB	Q9H4B4.
Enzyme and pathway databases
BRENDA	2.7.11.21. 2681.
Gene expression databases
ArrayExpress	Q9H4B4.
Bgee	Q9H4B4.
CleanEx	HS_PLK3.
Genevestigator	Q9H4B4.
GermOnline	ENSG00000173846. 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. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K08862.
Pfam	PF00069. Pkinase. 1 hit. PF00659. POLO_box. 2 hits. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50078. POLO_BOX. 2 hits. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	5111.
SOURCE	Search...

Entry information

Entry name

PLK3_HUMAN

Accession

Primary (citable) accession number: Q9H4B4
Secondary accession number(s): Q15767, Q5JR99, Q96CV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 111 of the entry and version 2 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.