PLK2_HUMAN
ID PLK2_HUMAN Reviewed; 685 AA.
AC Q9NYY3; O60679; Q96CV7; Q9UE61;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Serine/threonine-protein kinase PLK2;
DE EC=2.7.11.21;
DE AltName: Full=Polo-like kinase 2;
DE Short=PLK-2;
DE Short=hPlk2;
DE AltName: Full=Serine/threonine-protein kinase SNK;
DE Short=hSNK;
DE AltName: Full=Serum-inducible kinase;
GN Name=PLK2; Synonyms=SNK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11696980; DOI=10.3109/10425170109041337;
RA Liby K., Wu H., Ouyang B., Wu S., Chen J., Dai W.;
RT "Identification of the human homologue of the early-growth response gene
RT Snk, encoding a serum-inducible kinase.";
RL DNA Seq. 11:527-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RA Anderson K.M., Nerurkar S.S., Hansbury M.J., Fornwald J., Scott G.,
RA Bouzyk M., Mui P., Imbrugia C.S., Carlson K., Marshall L.A., Roshak A.K.;
RT "Identification and characterization of human serum-inducible kinase (SNK),
RT a novel member of the polo-kinase family of cell cycle regulators:
RT potential implication for regulation of vascular smooth muscle
RT proliferation.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 110-408.
RA Fidler C., Boultwood J., Wang Jabs E., Wainscoat J.S.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION.
RX PubMed=11716500; DOI=10.1006/bbrc.2001.5993;
RA Shimizu-Yoshida Y., Sugiyama K., Rogounovitch T., Ohtsuru A., Namba H.,
RA Saenko V., Yamashita S.;
RT "Radiation-inducible hSNK gene is transcriptionally regulated by p53
RT binding homology element in human thyroid cells.";
RL Biochem. Biophys. Res. Commun. 289:491-498(2001).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15242618; DOI=10.1016/j.cub.2004.06.059;
RA Warnke S., Kemmler S., Hames R.S., Tsai H.L., Hoffmann-Rohrer U., Fry A.M.,
RA Hoffmann I.;
RT "Polo-like kinase-2 is required for centriole duplication in mammalian
RT cells.";
RL Curr. Biol. 14:1200-1207(2004).
RN [8]
RP DOWN-REGULATION IN B-CELL LYMPHOMAS.
RX PubMed=16160013; DOI=10.1182/blood-2005-03-1194;
RA Syed N., Smith P., Sullivan A., Spender L.C., Dyer M., Karran L.,
RA O'Nions J., Allday M., Hoffmann I., Crawford D., Griffin B., Farrell P.J.,
RA Crook T.;
RT "Transcriptional silencing of Polo-like kinase 2 (SNK/PLK2) is a frequent
RT event in B-cell malignancies.";
RL Blood 107:250-256(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-210; TRP-503;
RP HIS-629 AND LYS-631.
RX PubMed=19001868; DOI=10.4161/cc.7.22.7071;
RA Cizmecioglu O., Warnke S., Arnold M., Duensing S., Hoffmann I.;
RT "Plk2 regulated centriole duplication is dependent on its localization to
RT the centrioles and a functional polo-box domain.";
RL Cell Cycle 7:3548-3555(2008).
RN [10]
RP INDUCTION.
RX PubMed=18832181; DOI=10.1073/pnas.0808266105;
RA Li Z., Lu J., Sun M., Mi S., Zhang H., Luo R.T., Chen P., Wang Y., Yan M.,
RA Qian Z., Neilly M.B., Jin J., Zhang Y., Bohlander S.K., Zhang D.E.,
RA Larson R.A., Le Beau M.M., Thirman M.J., Golub T.R., Rowley J.D., Chen J.;
RT "Distinct microRNA expression profiles in acute myeloid leukemia with
RT common translocations.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15535-15540(2008).
RN [11]
RP FUNCTION IN PHOSPHORYLATION OF CENPJ.
RX PubMed=20531387; DOI=10.1038/emboj.2010.118;
RA Chang J., Cizmecioglu O., Hoffmann I., Rhee K.;
RT "PLK2 phosphorylation is critical for CPAP function in procentriole
RT formation during the centrosome cycle.";
RL EMBO J. 29:2395-2406(2010).
RN [12]
RP FUNCTION IN PHOSPHORYLATION OF NPM.
RX PubMed=20352051; DOI=10.1371/journal.pone.0009849;
RA Krause A., Hoffmann I.;
RT "Polo-like kinase 2-dependent phosphorylation of NPM/B23 on serine 4
RT triggers centriole duplication.";
RL PLoS ONE 5:E9849-E9849(2010).
RN [13]
RP DOWN-REGULATION IN ACUTE MYELOID LEUKEMIA.
RX PubMed=21340720; DOI=10.1007/s00277-011-1193-4;
RA Benetatos L., Dasoula A., Hatzimichael E., Syed N., Voukelatou M.,
RA Dranitsaris G., Bourantas K.L., Crook T.;
RT "Polo-like kinase 2 (SNK/PLK2) is a novel epigenetically regulated gene in
RT acute myeloid leukemia and myelodysplastic syndromes: genetic and
RT epigenetic interactions.";
RL Ann. Hematol. 90:1037-1045(2011).
RN [14]
RP REVIEW ON FUNCTION.
RX PubMed=20671765; DOI=10.1038/nrd3184;
RA Strebhardt K.;
RT "Multifaceted polo-like kinases: drug targets and antitargets for cancer
RT therapy.";
RL Nat. Rev. Drug Discov. 9:643-660(2010).
RN [15]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-14; SER-92; LYS-436 AND LEU-487.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in
CC synaptic plasticity, centriole duplication and G1/S phase transition.
CC Polo-like kinases act by binding and phosphorylating proteins are that
CC already phosphorylated on a specific motif recognized by the POLO box
CC domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1
CC and SYNGAP1. Plays a key role in synaptic plasticity and memory by
CC regulating the Ras and Rap protein signaling: required for
CC overactivity-dependent spine remodeling by phosphorylating the Ras
CC activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their
CC degradation by the proteasome. Conversely, phosphorylates the Rap
CC activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their
CC activity. Also regulates synaptic plasticity independently of kinase
CC activity, via its interaction with NSF that disrupts the interaction
CC between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown
CC of AMPAR-mediated current that occludes long term depression. Required
CC for procentriole formation and centriole duplication by phosphorylating
CC CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that
CC it may participate in the mitotic checkpoint following stress.
CC {ECO:0000269|PubMed:15242618, ECO:0000269|PubMed:19001868,
CC ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:20531387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.21;
CC -!- ACTIVITY REGULATION: Activated by phosphorylation of Thr-239. Once
CC activated, activity is stimulated by binding target proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NSF; causing NSF dissociation from GRIA2.
CC Interacts with CIB1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NYY3; Q86Y33: CDC20B; NbExp=3; IntAct=EBI-721354, EBI-10260504;
CC Q9NYY3; Q9HC77: CENPJ; NbExp=3; IntAct=EBI-721354, EBI-946194;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:15242618,
CC ECO:0000269|PubMed:19001868}. Cell projection, dendrite {ECO:0000250}.
CC Note=Localizes to centrosomes during early G1 phase where it only
CC associates to the mother centriole and then distributes equally to both
CC mother and daughter centrioles at the onset of S phase.
CC -!- TISSUE SPECIFICITY: Expressed at higher level in the fetal lung,
CC kidney, spleen and heart. {ECO:0000269|PubMed:11696980}.
CC -!- INDUCTION: Directly regulated by p53/TP53. Negatively regulated by miR-
CC 126. {ECO:0000269|PubMed:11716500, ECO:0000269|PubMed:18832181}.
CC -!- DOMAIN: The POLO box domains act as phosphopeptide-binding module that
CC recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X)
CC motifs. PLK2 recognizes and binds docking proteins that are already
CC phosphorylated on these motifs, and then phosphorylates them (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Catalytic activity is enhanced by phosphorylation of Thr-239.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: There are indications that PLK2 might act as a tumor
CC suppressor: PLK2 is significantly down-regulated in a wide range of
CC acute myeloid leukemias (AMLs) and B-cell lymphomas due to aberrant
CC cytosine methylation in the CpG island located at the 5' of the PLK2
CC gene (PubMed:16160013, PubMed:21340720). Moreover, miR-126, a microRNA
CC that negatively regulates PLK2 is up-regulated in AMLs, suggesting that
CC PLK2 down-regulation by miR-126 could also contribute to leukemogenesis
CC (PubMed:18832181). {ECO:0000305|PubMed:16160013,
CC ECO:0000305|PubMed:18832181, ECO:0000305|PubMed:21340720}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AF059617; AAC14573.1; -; mRNA.
DR EMBL; AF223574; AAF62897.1; -; mRNA.
DR EMBL; U85755; AAD00575.1; -; mRNA.
DR EMBL; AC008814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013879; AAH13879.1; -; mRNA.
DR CCDS; CCDS3974.1; -.
DR RefSeq; NP_001239155.1; NM_001252226.1.
DR RefSeq; NP_006613.2; NM_006622.3.
DR PDB; 4I5M; X-ray; 1.80 A; A=57-360.
DR PDB; 4I5P; X-ray; 1.74 A; A=57-360.
DR PDB; 4I6B; X-ray; 1.80 A; A=57-360.
DR PDB; 4I6F; X-ray; 2.90 A; A=57-360.
DR PDB; 4I6H; X-ray; 1.91 A; A=57-360.
DR PDB; 4RS6; X-ray; 2.60 A; A/B=451-685.
DR PDB; 4XB0; X-ray; 2.70 A; A/B=468-685.
DR PDBsum; 4I5M; -.
DR PDBsum; 4I5P; -.
DR PDBsum; 4I6B; -.
DR PDBsum; 4I6F; -.
DR PDBsum; 4I6H; -.
DR PDBsum; 4RS6; -.
DR PDBsum; 4XB0; -.
DR AlphaFoldDB; Q9NYY3; -.
DR SMR; Q9NYY3; -.
DR BioGRID; 115988; 55.
DR DIP; DIP-48943N; -.
DR IntAct; Q9NYY3; 48.
DR MINT; Q9NYY3; -.
DR STRING; 9606.ENSP00000274289; -.
DR BindingDB; Q9NYY3; -.
DR ChEMBL; CHEMBL5938; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9NYY3; -.
DR GuidetoPHARMACOLOGY; 2169; -.
DR iPTMnet; Q9NYY3; -.
DR PhosphoSitePlus; Q9NYY3; -.
DR BioMuta; PLK2; -.
DR DMDM; 22096374; -.
DR MassIVE; Q9NYY3; -.
DR MaxQB; Q9NYY3; -.
DR PaxDb; Q9NYY3; -.
DR PeptideAtlas; Q9NYY3; -.
DR PRIDE; Q9NYY3; -.
DR ProteomicsDB; 83299; -.
DR Antibodypedia; 4042; 265 antibodies from 32 providers.
DR DNASU; 10769; -.
DR Ensembl; ENST00000274289.8; ENSP00000274289.3; ENSG00000145632.15.
DR GeneID; 10769; -.
DR KEGG; hsa:10769; -.
DR MANE-Select; ENST00000274289.8; ENSP00000274289.3; NM_006622.4; NP_006613.2.
DR UCSC; uc003jrn.4; human.
DR CTD; 10769; -.
DR DisGeNET; 10769; -.
DR GeneCards; PLK2; -.
DR HGNC; HGNC:19699; PLK2.
DR HPA; ENSG00000145632; Low tissue specificity.
DR MIM; 607023; gene.
DR neXtProt; NX_Q9NYY3; -.
DR OpenTargets; ENSG00000145632; -.
DR PharmGKB; PA134940798; -.
DR VEuPathDB; HostDB:ENSG00000145632; -.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000158739; -.
DR InParanoid; Q9NYY3; -.
DR OMA; MPEADSN; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; Q9NYY3; -.
DR TreeFam; TF101089; -.
DR BRENDA; 2.7.11.21; 2681.
DR PathwayCommons; Q9NYY3; -.
DR Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-HSA-9662834; CD163 mediating an anti-inflammatory response.
DR SignaLink; Q9NYY3; -.
DR SIGNOR; Q9NYY3; -.
DR BioGRID-ORCS; 10769; 11 hits in 1103 CRISPR screens.
DR ChiTaRS; PLK2; human.
DR GeneWiki; PLK2; -.
DR GenomeRNAi; 10769; -.
DR Pharos; Q9NYY3; Tchem.
DR PRO; PR:Q9NYY3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NYY3; protein.
DR Bgee; ENSG00000145632; Expressed in spleen and 194 other tissues.
DR ExpressionAtlas; Q9NYY3; baseline and differential.
DR Genevisible; Q9NYY3; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043008; F:ATP-dependent protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0060292; P:long-term synaptic depression; ISS:UniProtKB.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IDA:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0071866; P:negative regulation of apoptotic process in bone marrow cell; IEA:Ensembl.
DR GO; GO:2000773; P:negative regulation of cellular senescence; IEA:Ensembl.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; TAS:Reactome.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0046599; P:regulation of centriole replication; IDA:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR CDD; cd14188; STKc_PLK2; 1.
DR Gene3D; 3.30.1120.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042825; PLK2_STKc.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50078; POLO_BOX; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Tumor suppressor.
FT CHAIN 1..685
FT /note="Serine/threonine-protein kinase PLK2"
FT /id="PRO_0000086561"
FT DOMAIN 82..334
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 510..573
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 606..677
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 21..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 88..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53351"
FT VARIANT 14
FT /note="S -> T (in an ovarian Endometrioid carcinoma sample;
FT somatic mutation; dbSNP:rs1404394734)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041023"
FT VARIANT 92
FT /note="G -> S (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041024"
FT VARIANT 436
FT /note="E -> K (in dbSNP:rs55768901)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041025"
FT VARIANT 487
FT /note="P -> L (in dbSNP:rs55645589)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041026"
FT MUTAGEN 210
FT /note="N->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:19001868"
FT MUTAGEN 503
FT /note="W->F: Impairs localization to the centrosome and
FT centriole duplication; when associated with A-629 and M-
FT 631."
FT /evidence="ECO:0000269|PubMed:19001868"
FT MUTAGEN 629
FT /note="H->A: Impairs localization to the centrosome and
FT centriole duplication; when associated with F-503 and M-
FT 631."
FT /evidence="ECO:0000269|PubMed:19001868"
FT MUTAGEN 631
FT /note="K->M: Impairs localization to the centrosome and
FT centriole duplication; when associated with F-503 and A-
FT 631."
FT /evidence="ECO:0000269|PubMed:19001868"
FT CONFLICT 28
FT /note="A -> G (in Ref. 1; AAC14573)"
FT /evidence="ECO:0000305"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4I5P"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:4I5P"
FT STRAND 81..91
FT /evidence="ECO:0007829|PDB:4I5P"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:4I5P"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:4I5P"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:4I5P"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:4I5P"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 179..198
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:4I5P"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:4I5P"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:4I5M"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 325..329
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:4I5P"
FT HELIX 471..485
FT /evidence="ECO:0007829|PDB:4RS6"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:4XB0"
FT STRAND 504..510
FT /evidence="ECO:0007829|PDB:4RS6"
FT TURN 511..514
FT /evidence="ECO:0007829|PDB:4RS6"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:4RS6"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:4RS6"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:4RS6"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:4RS6"
FT STRAND 553..558
FT /evidence="ECO:0007829|PDB:4RS6"
FT HELIX 563..582
FT /evidence="ECO:0007829|PDB:4RS6"
FT STRAND 602..616
FT /evidence="ECO:0007829|PDB:4RS6"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:4RS6"
FT TURN 626..628
FT /evidence="ECO:0007829|PDB:4RS6"
FT STRAND 631..646
FT /evidence="ECO:0007829|PDB:4RS6"
FT STRAND 652..656
FT /evidence="ECO:0007829|PDB:4RS6"
FT HELIX 657..663
FT /evidence="ECO:0007829|PDB:4RS6"
FT HELIX 667..680
FT /evidence="ECO:0007829|PDB:4RS6"
SQ SEQUENCE 685 AA; 78237 MW; 6429F6EFD830B333 CRC64;
MELLRTITYQ PAASTKMCEQ ALGKGCGADS KKKRPPQPPE ESQPPQSQAQ VPPAAPHHHH
HHSHSGPEIS RIIVDPTTGK RYCRGKVLGK GGFAKCYEMT DLTNNKVYAA KIIPHSRVAK
PHQREKIDKE IELHRILHHK HVVQFYHYFE DKENIYILLE YCSRRSMAHI LKARKVLTEP
EVRYYLRQIV SGLKYLHEQE ILHRDLKLGN FFINEAMELK VGDFGLAARL EPLEHRRRTI
CGTPNYLSPE VLNKQGHGCE SDIWALGCVM YTMLLGRPPF ETTNLKETYR CIREARYTMP
SSLLAPAKHL IASMLSKNPE DRPSLDDIIR HDFFLQGFTP DRLSSSCCHT VPDFHLSSPA
KNFFKKAAAA LFGGKKDKAR YIDTHNRVSK EDEDIYKLRH DLKKTSITQQ PSKHRTDEEL
QPPTTTVARS GTPAVENKQQ IGDAIRMIVR GTLGSCSSSS ECLEDSTMGS VADTVARVLR
GCLENMPEAD CIPKEQLSTS FQWVTKWVDY SNKYGFGYQL SDHTVGVLFN NGAHMSLLPD
KKTVHYYAEL GQCSVFPATD APEQFISQVT VLKYFSHYME ENLMDGGDLP SVTDIRRPRL
YLLQWLKSDK ALMMLFNDGT FQVNFYHDHT KIIICSQNEE YLLTYINEDR ISTTFRLTTL
LMSGCSSELK NRMEYALNML LQRCN
