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Q9NYY3

- PLK2_HUMAN

UniProt

Q9NYY3 - PLK2_HUMAN

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Protein

Serine/threonine-protein kinase PLK2

Gene

PLK2

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

Functioni

Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by phosphorylation of Thr-239. Once activated, activity is stimulated by binding target proteins (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111ATPPROSITE-ProRule annotation
Active sitei205 – 2051Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 969ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB
  3. signal transducer activity Source: UniProtKB

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: UniProtKB
  2. long term synaptic depression Source: UniProtKB
  3. long-term synaptic potentiation Source: UniProtKB
  4. memory Source: UniProtKB
  5. mitotic cell cycle checkpoint Source: UniProtKB
  6. mitotic spindle organization Source: UniProtKB
  7. negative regulation of apoptotic process Source: UniProtKB
  8. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  9. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  10. protein phosphorylation Source: UniProtKB
  11. Rap protein signal transduction Source: UniProtKB
  12. Ras protein signal transduction Source: UniProtKB
  13. regulation of centriole replication Source: UniProtKB
  14. regulation of synaptic plasticity 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.
SignaLinkiQ9NYY3.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PLK2 (EC:2.7.11.21)
Alternative name(s):
Polo-like kinase 2
Short name:
PLK-2
Short name:
hPlk2
Serine/threonine-protein kinase SNK
Short name:
hSNK
Serum-inducible kinase
Gene namesi
Name:PLK2
Synonyms:SNK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:19699. PLK2.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole 2 Publications. Cell projectiondendrite By similarity
Note: Localizes to centrosomes during early G1 phase where it only associates to the mother centriole and then distributes equally to both mother and daughter centrioles at the onset of S phase.

GO - Cellular componenti

  1. centriole Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. dendrite Source: UniProtKB
  4. intracellular Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi210 – 2101N → A: Loss of kinase activity. 1 Publication
Mutagenesisi503 – 5031W → F: Impairs localization to the centrosome and centriole duplication; when associated with A-629 and M-631. 1 Publication
Mutagenesisi629 – 6291H → A: Impairs localization to the centrosome and centriole duplication; when associated with F-503 and M-631. 1 Publication
Mutagenesisi631 – 6311K → M: Impairs localization to the centrosome and centriole duplication; when associated with F-503 and A-631. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA134940798.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 685685Serine/threonine-protein kinase PLK2PRO_0000086561Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391PhosphothreonineBy similarity

Post-translational modificationi

Catalytic activity is enhanced by phosphorylation of Thr-239.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NYY3.
PaxDbiQ9NYY3.
PRIDEiQ9NYY3.

PTM databases

PhosphoSiteiQ9NYY3.

Expressioni

Tissue specificityi

Expressed at higher level in the fetal lung, kidney, spleen and heart.1 Publication

Inductioni

Directly regulated by p53/TP53. Negatively regulated by miR-126.2 Publications

Gene expression databases

BgeeiQ9NYY3.
CleanExiHS_PLK2.
GenevestigatoriQ9NYY3.

Organism-specific databases

HPAiCAB009624.

Interactioni

Subunit structurei

Interacts with NSF; causing NSF dissociation from GRIA2. Interacts with CIB1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CENPJQ9HC773EBI-721354,EBI-946194

Protein-protein interaction databases

BioGridi115988. 33 interactions.
DIPiDIP-48943N.
IntActiQ9NYY3. 8 interactions.
MINTiMINT-1397390.
STRINGi9606.ENSP00000274289.

Structurei

Secondary structure

1
685
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi72 – 743
Turni76 – 783
Beta strandi81 – 9111
Beta strandi94 – 1018
Turni102 – 1054
Beta strandi106 – 1149
Helixi115 – 1184
Helixi121 – 13414
Beta strandi145 – 1506
Beta strandi152 – 1598
Helixi167 – 1748
Helixi179 – 19820
Helixi208 – 2103
Beta strandi211 – 2133
Beta strandi219 – 2213
Helixi224 – 2263
Turni233 – 2353
Helixi249 – 2524
Helixi259 – 27517
Helixi286 – 2883
Helixi289 – 2935
Helixi305 – 31410
Helixi319 – 3213
Helixi325 – 3295
Helixi332 – 3354
Helixi345 – 3484

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I5MX-ray1.80A57-360[»]
4I5PX-ray1.74A57-360[»]
4I6BX-ray1.80A57-360[»]
4I6FX-ray2.90A57-360[»]
4I6HX-ray1.91A57-360[»]
ProteinModelPortaliQ9NYY3.
SMRiQ9NYY3. Positions 71-354, 503-680.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 334253Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini510 – 57364POLO box 1PROSITE-ProRule annotationAdd
BLAST
Domaini606 – 67772POLO box 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi57 – 648Poly-His

Domaini

The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK2 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them (By similarity).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

eggNOGiCOG0515.
GeneTreeiENSGT00530000062954.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiQ9NYY3.
KOiK08861.
OMAiRHEFFLQ.
OrthoDBiEOG78M01K.
PhylomeDBiQ9NYY3.
TreeFamiTF101089.

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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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.

Q9NYY3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELLRTITYQ PAASTKMCEQ ALGKGCGADS KKKRPPQPPE ESQPPQSQAQ
60 70 80 90 100
VPPAAPHHHH HHSHSGPEIS RIIVDPTTGK RYCRGKVLGK GGFAKCYEMT
110 120 130 140 150
DLTNNKVYAA KIIPHSRVAK PHQREKIDKE IELHRILHHK HVVQFYHYFE
160 170 180 190 200
DKENIYILLE YCSRRSMAHI LKARKVLTEP EVRYYLRQIV SGLKYLHEQE
210 220 230 240 250
ILHRDLKLGN FFINEAMELK VGDFGLAARL EPLEHRRRTI CGTPNYLSPE
260 270 280 290 300
VLNKQGHGCE SDIWALGCVM YTMLLGRPPF ETTNLKETYR CIREARYTMP
310 320 330 340 350
SSLLAPAKHL IASMLSKNPE DRPSLDDIIR HDFFLQGFTP DRLSSSCCHT
360 370 380 390 400
VPDFHLSSPA KNFFKKAAAA LFGGKKDKAR YIDTHNRVSK EDEDIYKLRH
410 420 430 440 450
DLKKTSITQQ PSKHRTDEEL QPPTTTVARS GTPAVENKQQ IGDAIRMIVR
460 470 480 490 500
GTLGSCSSSS ECLEDSTMGS VADTVARVLR GCLENMPEAD CIPKEQLSTS
510 520 530 540 550
FQWVTKWVDY SNKYGFGYQL SDHTVGVLFN NGAHMSLLPD KKTVHYYAEL
560 570 580 590 600
GQCSVFPATD APEQFISQVT VLKYFSHYME ENLMDGGDLP SVTDIRRPRL
610 620 630 640 650
YLLQWLKSDK ALMMLFNDGT FQVNFYHDHT KIIICSQNEE YLLTYINEDR
660 670 680
ISTTFRLTTL LMSGCSSELK NRMEYALNML LQRCN
Length:685
Mass (Da):78,237
Last modified:August 2, 2002 - v3
Checksum:i6429F6EFD830B333
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281A → G in AAC14573. (PubMed:11696980)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141S → T in an ovarian Endometrioid carcinoma sample; somatic mutation. 1 Publication
VAR_041023
Natural varianti92 – 921G → S in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041024
Natural varianti436 – 4361E → K.1 Publication
Corresponds to variant rs55768901 [ dbSNP | Ensembl ].
VAR_041025
Natural varianti487 – 4871P → L.1 Publication
Corresponds to variant rs55645589 [ dbSNP | Ensembl ].
VAR_041026

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF059617 mRNA. Translation: AAC14573.1.
AF223574 mRNA. Translation: AAF62897.1.
U85755 mRNA. Translation: AAD00575.1.
AC008814 Genomic DNA. No translation available.
BC013879 mRNA. Translation: AAH13879.1.
CCDSiCCDS3974.1.
RefSeqiNP_001239155.1. NM_001252226.1.
NP_006613.2. NM_006622.3.
UniGeneiHs.398157.

Genome annotation databases

EnsembliENST00000274289; ENSP00000274289; ENSG00000145632.
GeneIDi10769.
KEGGihsa:10769.
UCSCiuc003jrn.3. human.

Polymorphism databases

DMDMi22096374.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF059617 mRNA. Translation: AAC14573.1 .
AF223574 mRNA. Translation: AAF62897.1 .
U85755 mRNA. Translation: AAD00575.1 .
AC008814 Genomic DNA. No translation available.
BC013879 mRNA. Translation: AAH13879.1 .
CCDSi CCDS3974.1.
RefSeqi NP_001239155.1. NM_001252226.1.
NP_006613.2. NM_006622.3.
UniGenei Hs.398157.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4I5M X-ray 1.80 A 57-360 [» ]
4I5P X-ray 1.74 A 57-360 [» ]
4I6B X-ray 1.80 A 57-360 [» ]
4I6F X-ray 2.90 A 57-360 [» ]
4I6H X-ray 1.91 A 57-360 [» ]
ProteinModelPortali Q9NYY3.
SMRi Q9NYY3. Positions 71-354, 503-680.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115988. 33 interactions.
DIPi DIP-48943N.
IntActi Q9NYY3. 8 interactions.
MINTi MINT-1397390.
STRINGi 9606.ENSP00000274289.

Chemistry

BindingDBi Q9NYY3.
ChEMBLi CHEMBL5938.
GuidetoPHARMACOLOGYi 2169.

PTM databases

PhosphoSitei Q9NYY3.

Polymorphism databases

DMDMi 22096374.

Proteomic databases

MaxQBi Q9NYY3.
PaxDbi Q9NYY3.
PRIDEi Q9NYY3.

Protocols and materials databases

DNASUi 10769.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274289 ; ENSP00000274289 ; ENSG00000145632 .
GeneIDi 10769.
KEGGi hsa:10769.
UCSCi uc003jrn.3. human.

Organism-specific databases

CTDi 10769.
GeneCardsi GC05M057749.
HGNCi HGNC:19699. PLK2.
HPAi CAB009624.
MIMi 607023. gene.
neXtProti NX_Q9NYY3.
PharmGKBi PA134940798.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000062954.
HOGENOMi HOG000248546.
HOVERGENi HBG001843.
InParanoidi Q9NYY3.
KOi K08861.
OMAi RHEFFLQ.
OrthoDBi EOG78M01K.
PhylomeDBi Q9NYY3.
TreeFami TF101089.

Enzyme and pathway databases

BRENDAi 2.7.11.21. 2681.
SignaLinki Q9NYY3.

Miscellaneous databases

GeneWikii PLK2.
GenomeRNAii 10769.
NextBioi 40893.
PROi Q9NYY3.
SOURCEi Search...

Gene expression databases

Bgeei Q9NYY3.
CleanExi HS_PLK2.
Genevestigatori Q9NYY3.

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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the human homologue of the early-growth response gene Snk, encoding a serum-inducible kinase."
    Liby K., Wu H., Ouyang B., Wu S., Chen J., Dai W.
    DNA Seq. 11:527-533(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Identification and characterization of human serum-inducible kinase (SNK), a novel member of the polo-kinase family of cell cycle regulators: potential implication for regulation of vascular smooth muscle proliferation."
    Anderson K.M., Nerurkar S.S., Hansbury M.J., Fornwald J., Scott G., Bouzyk M., Mui P., Imbrugia C.S., Carlson K., Marshall L.A., Roshak A.K.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Skin.
  5. Fidler C., Boultwood J., Wang Jabs E., Wainscoat J.S.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-408.
  6. "Radiation-inducible hSNK gene is transcriptionally regulated by p53 binding homology element in human thyroid cells."
    Shimizu-Yoshida Y., Sugiyama K., Rogounovitch T., Ohtsuru A., Namba H., Saenko V., Yamashita S.
    Biochem. Biophys. Res. Commun. 289:491-498(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "Polo-like kinase-2 is required for centriole duplication in mammalian cells."
    Warnke S., Kemmler S., Hames R.S., Tsai H.L., Hoffmann-Rohrer U., Fry A.M., Hoffmann I.
    Curr. Biol. 14:1200-1207(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Transcriptional silencing of Polo-like kinase 2 (SNK/PLK2) is a frequent event in B-cell malignancies."
    Syed N., Smith P., Sullivan A., Spender L.C., Dyer M., Karran L., O'Nions J., Allday M., Hoffmann I., Crawford D., Griffin B., Farrell P.J., Crook T.
    Blood 107:250-256(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-REGULATION IN B-CELL LYMPHOMAS.
  9. "Plk2 regulated centriole duplication is dependent on its localization to the centrioles and a functional polo-box domain."
    Cizmecioglu O., Warnke S., Arnold M., Duensing S., Hoffmann I.
    Cell Cycle 7:3548-3555(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-210; TRP-503; HIS-629 AND LYS-631.
  10. Cited for: INDUCTION.
  11. "PLK2 phosphorylation is critical for CPAP function in procentriole formation during the centrosome cycle."
    Chang J., Cizmecioglu O., Hoffmann I., Rhee K.
    EMBO J. 29:2395-2406(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CENPJ.
  12. "Polo-like kinase 2-dependent phosphorylation of NPM/B23 on serine 4 triggers centriole duplication."
    Krause A., Hoffmann I.
    PLoS ONE 5:E9849-E9849(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF NPM.
  13. "Polo-like kinase 2 (SNK/PLK2) is a novel epigenetically regulated gene in acute myeloid leukemia and myelodysplastic syndromes: genetic and epigenetic interactions."
    Benetatos L., Dasoula A., Hatzimichael E., Syed N., Voukelatou M., Dranitsaris G., Bourantas K.L., Crook T.
    Ann. Hematol. 90:1037-1045(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-REGULATION IN ACUTE MYELOID LEUKEMIA.
  14. "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.
  15. "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] THR-14; SER-92; LYS-436 AND LEU-487.

Entry informationi

Entry nameiPLK2_HUMAN
AccessioniPrimary (citable) accession number: Q9NYY3
Secondary accession number(s): O60679, Q96CV7, Q9UE61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 2, 2002
Last modified: October 29, 2014
This is version 136 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

Miscellaneous

There are indications that PLK2 might act as a tumor suppressor: PLK2 is significantly down-regulated in a wide range of acute myeloid leukemias (AMLs) and B-cell lymphomas due to aberrant cytosine methylation in the CpG island located at the 5' of the PLK2 gene (PubMed:16160013, PubMed:21340720). Moreover, miR-126, a microRNA that negatively regulates PLK2 is up-regulated in AMLs, suggesting that PLK2 down-regulation by miR-126 could also contribute to leukemogenesis (PubMed:18832181).3 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

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