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Serine/threonine-protein kinase PLK2 (EC 2.7.11.21) (Polo-like kinase 2) (PLK-2) (Serine/threonine-protein kinase SNK) (Serum-inducible kinase)

 PLK2_MOUSE              Reviewed;         682 AA.
P53351;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
10-MAY-2017, entry version 146.
RecName: Full=Serine/threonine-protein kinase PLK2;
EC=2.7.11.21;
AltName: Full=Polo-like kinase 2;
Short=PLK-2;
AltName: Full=Serine/threonine-protein kinase SNK;
AltName: Full=Serum-inducible kinase;
Name=Plk2; Synonyms=Snk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
PubMed=1508211; DOI=10.1128/MCB.12.9.4164;
Simmons D.L., Neel B.G., Stevens R., Evett G., Erikson R.L.;
"Identification of an early-growth-response gene encoding a novel
putative protein kinase.";
Mol. Cell. Biol. 12:4164-4169(1992).
[2]
FUNCTION, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT THR-236, AND
MUTAGENESIS OF LYS-108 AND THR-236.
PubMed=12651910;
Ma S., Liu M.A., Yuan Y.L., Erikson R.L.;
"The serum-inducible protein kinase Snk is a G1 phase polo-like kinase
that is inhibited by the calcium- and integrin-binding protein CIB.";
Mol. Cancer Res. 1:376-384(2003).
[3]
FUNCTION, INDUCTION, AND MUTAGENESIS OF THR-236.
PubMed=12897130; DOI=10.1128/MCB.23.16.5556-5571.2003;
Burns T.F., Fei P., Scata K.A., Dicker D.T., El-Deiry W.S.;
"Silencing of the novel p53 target gene Snk/Plk2 leads to mitotic
catastrophe in paclitaxel (taxol)-exposed cells.";
Mol. Cell. Biol. 23:5556-5571(2003).
[4]
DISRUPTION PHENOTYPE.
PubMed=12972611; DOI=10.1128/MCB.23.19.6936-6943.2003;
Ma S., Charron J., Erikson R.L.;
"Role of Plk2 (Snk) in mouse development and cell proliferation.";
Mol. Cell. Biol. 23:6936-6943(2003).
[5]
FUNCTION IN PHOSPHORYLATION OF SNCA.
PubMed=19004816; DOI=10.1074/jbc.C800206200;
Inglis K.J., Chereau D., Brigham E.F., Chiou S.S., Schobel S.,
Frigon N.L., Yu M., Caccavello R.J., Nelson S., Motter R., Wright S.,
Chian D., Santiago P., Soriano F., Ramos C., Powell K.,
Goldstein J.M., Babcock M., Yednock T., Bard F., Basi G.S., Sham H.,
Chilcote T.J., McConlogue L., Griswold-Prenner I., Anderson J.P.;
"Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine
129 in central nervous system.";
J. Biol. Chem. 284:2598-2602(2009).
[6]
FUNCTION, MUTAGENESIS OF LYS-108, AND DISRUPTION PHENOTYPE.
PubMed=21382555; DOI=10.1016/j.neuron.2011.02.004;
Lee K.J., Lee Y., Rozeboom A., Lee J.Y., Udagawa N., Hoe H.S.,
Pak D.T.;
"Requirement for Plk2 in orchestrated ras and rap signaling,
homeostatic structural plasticity, and memory.";
Neuron 69:957-973(2011).
-!- FUNCTION: 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. {ECO:0000269|PubMed:12651910,
ECO:0000269|PubMed:12897130, ECO:0000269|PubMed:19004816,
ECO:0000269|PubMed:21382555}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by phosphorylation of Thr-236. Once
activated, activity is stimulated by binding target proteins (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with NSF; causing NSF dissociation from GRIA2
(By similarity). Interacts with CIB1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole {ECO:0000250}. Cell
projection, dendrite {ECO:0000250}. 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. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Brain, lung and heart.
{ECO:0000269|PubMed:1508211}.
-!- DEVELOPMENTAL STAGE: Expressed in early G1, during G0-G1
transition as well as in cycling cells.
{ECO:0000269|PubMed:12651910}.
-!- INDUCTION: Directly regulated by p53/TP53. Induced by serum and
phorbol ester. {ECO:0000269|PubMed:12897130,
ECO:0000269|PubMed:1508211}.
-!- DOMAIN: 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). {ECO:0000250}.
-!- PTM: Catalytic activity is enhanced by phosphorylation of Thr-236.
{ECO:0000269|PubMed:12651910}.
-!- DISRUPTION PHENOTYPE: Embryos display a delay in skeletal
development and retarded growth. Embryonic fibroblasts
proliferated slowly and displayed a delayed entry into S phase.
Mice display loss of dendritic spines and impaired memory
formation. {ECO:0000269|PubMed:12972611,
ECO:0000269|PubMed:21382555}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; M96163; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS26767.1; -.
PIR; A44493; A44493.
RefSeq; NP_690017.2; NM_152804.2.
UniGene; Mm.380; -.
ProteinModelPortal; P53351; -.
SMR; P53351; -.
BioGrid; 203368; 10.
IntAct; P53351; 9.
STRING; 10090.ENSMUSP00000022212; -.
iPTMnet; P53351; -.
PhosphoSitePlus; P53351; -.
PaxDb; P53351; -.
PRIDE; P53351; -.
Ensembl; ENSMUST00000022212; ENSMUSP00000022212; ENSMUSG00000021701.
GeneID; 20620; -.
KEGG; mmu:20620; -.
UCSC; uc007rvs.2; mouse.
CTD; 10769; -.
MGI; MGI:1099790; Plk2.
eggNOG; KOG0575; Eukaryota.
eggNOG; ENOG410XQBP; LUCA.
GeneTree; ENSGT00530000062954; -.
HOGENOM; HOG000248546; -.
HOVERGEN; HBG001843; -.
InParanoid; P53351; -.
KO; K08861; -.
OMA; NGTHMSL; -.
OrthoDB; EOG091G0D89; -.
PhylomeDB; P53351; -.
TreeFam; TF101089; -.
BRENDA; 2.7.11.21; 3474.
Reactome; R-MMU-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
PRO; PR:P53351; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021701; -.
CleanEx; MM_PLK2; -.
ExpressionAtlas; P53351; baseline and differential.
Genevisible; P53351; MM.
GO; GO:0005814; C:centriole; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0000785; C:chromatin; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043008; F:ATP-dependent protein binding; ISO:MGI.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0004871; F:signal transducer activity; ISO:MGI.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0060292; P:long term synaptic depression; ISS:UniProtKB.
GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
GO; GO:0007613; P:memory; IMP:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IMP:UniProtKB.
GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0061000; P:negative regulation of dendritic spine development; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
CDD; cd13118; POLO_box_1; 1.
CDD; cd13117; POLO_box_2; 1.
Gene3D; 3.30.1120.30; -; 2.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR033701; POLO_box_1.
InterPro; IPR033695; POLO_box_2.
InterPro; IPR000959; POLO_box_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00659; POLO_box; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50078; POLO_BOX; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell projection; Complete proteome; Cytoplasm;
Cytoskeleton; Kinase; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase; Tumor suppressor.
CHAIN 1 682 Serine/threonine-protein kinase PLK2.
/FTId=PRO_0000086562.
DOMAIN 79 331 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 507 570 POLO box 1. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
DOMAIN 603 674 POLO box 2. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
NP_BIND 85 93 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 54 59 Poly-His.
ACT_SITE 202 202 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 108 108 ATP. {ECO:0000305}.
MOD_RES 236 236 Phosphothreonine.
{ECO:0000269|PubMed:12651910}.
MUTAGEN 108 108 K->M: In DN mutant; Loss of kinase
activity; leading to disrupted Ras and
Rap protein signaling, altered spine
morphology and aberrant memory formation
in mice. {ECO:0000269|PubMed:12651910,
ECO:0000269|PubMed:21382555}.
MUTAGEN 236 236 T->D,V: Does not significantely affect
kinase activity.
{ECO:0000269|PubMed:12651910,
ECO:0000269|PubMed:12897130}.
MUTAGEN 236 236 T->E: Mimicks phosphorylation state,
leading to increased activity.
{ECO:0000269|PubMed:12651910,
ECO:0000269|PubMed:12897130}.
SEQUENCE 682 AA; 77812 MW; 586DEABFD7208A9D CRC64;
MELLRTITYQ PAAGTKMCEQ ALGKACGGDS KKKRPQQPSE DGQPQAQVTP AAPHHHHHHS
HSGPEISRII VDPTTGKRYC RGKVLGKGGF AKCYEMTDLT NNKVYAAKII PHSRVAKPHQ
REKIDKEIEL HRLLHHKHVV 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 KVSITQQPSK HRADEEPQPP
PTTVARSGTS AVENKQQIGD AIRMIVRGTL GSCSSSSECL EDSTMGSVAD TVARVLRGCL
ENMPEADCIP KEQLSTSFQW VTKWVDYSNK YGFGYQLSDH TVGVLFNNGA HMSLLPDKKT
VHYYAELGQC SVFPATDAPE QFISQVTVLK YFSHYMEENL MDGGDLPSVT DIRRPRLYLL
QWLKSDKALM MLFNDGTFQV NFYHDHTKII ICNQSEEYLL TYINEDRIST TFRLTTLLMS
GCSLELKNRM EYALNMLLQR CN


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