Reviewed, UniProtKB/Swiss-Prot Q9H4B4 (PLK3_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase PLK3
    EC=2.7.11.21
Alternative name(s):
    Polo-like kinase 3
      Short name=PLK-3
    Cytokine-inducible serine/threonine-protein kinase
    FGF-inducible kinase
    Proliferation-related kinase

Gene names

Name:	PLK3
Synonyms:	CNK, FNK, PRK

Organism

Homo sapiens (Human) [Complete proteome]

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 regulating M phase functions during the cell cycle. May also be part of the signaling network controlling cellular adhesion. In vitro, is able to phosphorylate CDC25C and casein.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Binds to the calcium/integrin-binding protein (CIB). This interaction probably occurs via the POLO-box domain.
Subcellular location	Membrane; Peripheral membrane protein.
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.
Induction	Cytokine and cellular adhesion trigger FNK induction.
Post-translational modification	Phosphorylated as cells enter mitosis and dephosphorylated as cells exit mitosis By similarity. Ref.9
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.

Ontologies

Keywords
Cellular component	Membrane
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
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: InterPro protein amino acid phosphorylation Ref.6 Traceable author statement. Source: ProtInc
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW polo kinase kinase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VRK1	Q99986	6	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	348	1	Phosphothreonine Ref.9
Natural variations
	Natural variant	61	1	T → S: dbSNP rs17884581. Ref.2		VAR_021091
	Natural variant	68	1	L → F: dbSNP rs17884316. Ref.2		VAR_021092
	Natural variant	283	1	L → F: dbSNP rs17880471. Ref.2		VAR_021093
	Natural variant	483	1	R → C: dbSNP rs17884653. Ref.2		VAR_021094
	Natural variant	491	1	D → N: dbSNP rs17855444.		VAR_062384
	Natural variant	498	1	S → L: dbSNP rs17880829. Ref.2		VAR_021095
	Natural variant	618	1	S → P: dbSNP rs17881786. Ref.2		VAR_021096
Experimental info
	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)
	Q9H4B4-1 [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]	"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: CHARACTERIZATION.
[8]	"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: CHARACTERIZATION.
[9]	"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.
+	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.
UniGene	Hs.632415
3D structure databases
SMR	Q9H4B4. Positions 52-329, 458-642.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H4B4. 3 interactions.
STRING	Q9H4B4.
Proteomic databases
PRIDE	Q9H4B4.
Genome annotation databases
Ensembl	ENST00000372201; ENSP00000361275; ENSG00000173846; Homo sapiens. [Genome view]
GeneID	1263.
KEGG	hsa:1263.
UCSC	uc001cmn.1. human.
Organism-specific databases
CTD	1263.
GeneCards	GC01P045038.
H-InvDB	HIX0000520.
HGNC	HGNC:2154. PLK3.
MIM	602913. gene.
PharmGKB	PA26664.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10409.
HOGENOM	HBG738952.
HOVERGEN	Q9H4B4.
InParanoid	Q9H4B4.
OMA	PRSGRTY.
OrthoDB	EOG9NW252.
PhylomeDB	Q9H4B4.
Enzyme and pathway databases
BRENDA	2.7.11.21. 247.
Gene expression databases
ArrayExpress	Q9H4B4.
Bgee	Q9H4B4.
CleanEx	HS_PLK3.
Genevestigator	Q9H4B4.
GermOnline	ENSG00000173846. Homo sapiens.
Family and domain databases
InterPro	IPR020636. Ca/CaM-dep_prot_kinase-like. IPR011009. Kinase-like_dom. IPR000959. POLO_box_duplicated_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. IPR015728. Ser/Thr_prot_kinase_Polo-like. [Graphical view]
PANTHER	PTHR22982. Ca/CaM-dep_prot_kinase-like. 1 hit. PTHR22982:SF10. Polo-like_kinase. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. PF00659. POLO_box. 2 hits. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
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 Resources
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:	February 9, 2010
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.