PLK2_RAT
ID PLK2_RAT Reviewed; 682 AA.
AC Q9R012;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
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 AltName: Full=Serine/threonine-protein kinase SNK;
DE AltName: Full=Serum-inducible kinase;
GN Name=Plk2; Synonyms=Snk;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH CIB1.
RX PubMed=10523297; DOI=10.1093/emboj/18.20.5528;
RA Kauselmann G., Weiler M., Wulff P., Jessberger S., Konietzko U.,
RA Scafidi J., Staubli U., Bereiter-Hahn J., Strebhardt K., Kuhl D.;
RT "The polo-like protein kinases Fnk and Snk associate with a Ca(2+)- and
RT integrin-binding protein and are regulated dynamically with synaptic
RT plasticity.";
RL EMBO J. 18:5528-5539(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP FUNCTION IN PHOSPHORYLATION OF SIPA1L1, AND MUTAGENESIS OF ASP-202.
RX PubMed=18723513; DOI=10.1074/jbc.m802475200;
RA Ang X.L., Seeburg D.P., Sheng M., Harper J.W.;
RT "Regulation of postsynaptic RapGAP SPAR by Polo-like kinase 2 and the
RT SCFbeta-TRCP ubiquitin ligase in hippocampal neurons.";
RL J. Biol. Chem. 283:29424-29432(2008).
RN [4]
RP FUNCTION IN PHOSPHORYLATION OF SIPA1L1, AND MUTAGENESIS OF TRP-504.
RX PubMed=18498738; DOI=10.1016/j.neuron.2008.03.021;
RA Seeburg D.P., Feliu-Mojer M., Gaiottino J., Pak D.T., Sheng M.;
RT "Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic
RT plasticity during elevated activity.";
RL Neuron 58:571-583(2008).
RN [5]
RP FUNCTION, INTERACTION WITH NSF, PHOSPHORYLATION AT THR-236, AND MUTAGENESIS
RP OF LYS-108; THR-236 AND TRP-504.
RX PubMed=20802490; DOI=10.1038/nn.2624;
RA Evers D.M., Matta J.A., Hoe H.S., Zarkowsky D., Lee S.H., Isaac J.T.,
RA Pak D.T.;
RT "Plk2 attachment to NSF induces homeostatic removal of GluA2 during chronic
RT overexcitation.";
RL Nat. Neurosci. 13:1199-1207(2010).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF LYS-108 AND THR-236.
RX PubMed=21382555; DOI=10.1016/j.neuron.2011.02.004;
RA Lee K.J., Lee Y., Rozeboom A., Lee J.Y., Udagawa N., Hoe H.S., Pak D.T.;
RT "Requirement for Plk2 in orchestrated ras and rap signaling, homeostatic
RT structural plasticity, and memory.";
RL Neuron 69:957-973(2011).
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:10523297, ECO:0000269|PubMed:18498738,
CC ECO:0000269|PubMed:18723513, ECO:0000269|PubMed:20802490,
CC ECO:0000269|PubMed:21382555}.
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-236. Once
CC activated, activity is stimulated by binding target proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CIB1 (By similarity). Interacts with NSF;
CC causing NSF dissociation from GRIA2. {ECO:0000250,
CC ECO:0000269|PubMed:10523297, ECO:0000269|PubMed:20802490}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000269|PubMed:10523297}. Note=Localizes to centrosomes during
CC early G1 phase where it only associates to the mother centriole and
CC then distributes equally to both mother and daughter centrioles at the
CC onset of S phase. {ECO:0000250}.
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-236.
CC {ECO:0000269|PubMed:20802490}.
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; AF136583; AAF08366.1; -; mRNA.
DR EMBL; BC070878; AAH70878.1; -; mRNA.
DR RefSeq; NP_114009.1; NM_031821.1.
DR AlphaFoldDB; Q9R012; -.
DR SMR; Q9R012; -.
DR BioGRID; 249816; 5.
DR IntAct; Q9R012; 1.
DR MINT; Q9R012; -.
DR STRING; 10116.ENSRNOP00000016768; -.
DR iPTMnet; Q9R012; -.
DR PhosphoSitePlus; Q9R012; -.
DR PaxDb; Q9R012; -.
DR Ensembl; ENSRNOT00000016768; ENSRNOP00000016768; ENSRNOG00000011951.
DR GeneID; 83722; -.
DR KEGG; rno:83722; -.
DR CTD; 10769; -.
DR RGD; 620760; Plk2.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000158739; -.
DR HOGENOM; CLU_000288_46_1_1; -.
DR InParanoid; Q9R012; -.
DR OMA; MPEADSN; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; Q9R012; -.
DR TreeFam; TF101089; -.
DR BRENDA; 2.7.11.21; 5301.
DR Reactome; R-RNO-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR PRO; PR:Q9R012; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011951; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q9R012; RN.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA: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; ISO:RGD.
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:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0060292; P:long-term synaptic depression; IDA:UniProtKB.
DR GO; GO:0060291; P:long-term synaptic potentiation; IDA:UniProtKB.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:RGD.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
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; ISO:RGD.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISO:RGD.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; IMP:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:RGD.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0032486; P:Rap protein signal transduction; IDA:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:UniProtKB.
DR GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IDA: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 ATP-binding; Cell projection; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Tumor suppressor.
FT CHAIN 1..682
FT /note="Serine/threonine-protein kinase PLK2"
FT /id="PRO_0000086563"
FT DOMAIN 79..331
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 507..570
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 603..674
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 25..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 85..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20802490"
FT MUTAGEN 108
FT /note="K->M: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:20802490,
FT ECO:0000269|PubMed:21382555"
FT MUTAGEN 202
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:18723513"
FT MUTAGEN 236
FT /note="T->E: Mimicks phosphorylation state, leading to
FT increased activity."
FT /evidence="ECO:0000269|PubMed:20802490,
FT ECO:0000269|PubMed:21382555"
FT MUTAGEN 504
FT /note="W->A: Abolishes interaction with SIPA1L1."
FT /evidence="ECO:0000269|PubMed:18498738,
FT ECO:0000269|PubMed:20802490"
FT MUTAGEN 504
FT /note="W->F: Does not affect interaction with NSF and
FT ability to dissociate NSF from GRIA2."
FT /evidence="ECO:0000269|PubMed:18498738,
FT ECO:0000269|PubMed:20802490"
SQ SEQUENCE 682 AA; 77920 MW; 58C50DEBDE83D5F3 CRC64;
MELLRTITYQ PAAGTKMCEQ ALGKACGGDS KKKRPQQPSE DGQSQAQVTP AAPHHHHHHS
HSGPEISRII VDPTTGKRYC RGKVLGKGGF AKCYEMTDLT NNKVYAAKII PHSRVAKPHQ
REKIDKEIEL HRILHHKHVV QFYHYFEDKE NIYILLEYCS RRSMAHILKA RKVLTEPEVR
YYLRQIVSGL KYLHEQEILH RDLKLGNFFI NEAMELKVGD FGLAARLEPL EHRRRTICGT
PNYLSPEVLN KQGHGCESDI WALGCVMYTM LLGRPPFETT NLKETYRCIR EARYTMPSSL
LAPAKHLIAS MLSKNPEDRP SLDDIIRHDF FLQGFTPDRL SSSCCHTVPD FHLSSPAKNF
FKKAAAALFG GKKDKARYND THNKVSKEDE DIYKLRHDLK KTSITQQPSK HRTDEELQPP
PTTFAKSGTS AVENKQQIGD AIRMIVRGTL GSCSSSSECL EDSTMGSVAD TVARVLRGCL
ENMPEADCIP KEQLSTSFQW VTKWVDYSNK YGFGYQLSDH TVGVLFNNGA HMSLLPDKKT
VHYYAELGQC SVFPATDAPE QFISQVTVLK YFSHYMEENL MDGGDLPSVT DIRRPRLYLL
QWLKSDKALM MLFNDGTFQV NFYHDHTKII ICNQNEEYLL TYINEDRIST TFRLTTLLMS
GCSLELKHRM EYALNMLLQR CN
