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Protein

Serine/threonine-protein kinase PLK2

Gene

Plk2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by phosphorylation of Thr-236. Once activated, activity is stimulated by binding target proteins (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei108 – 1081ATP
Active sitei202 – 2021Proton acceptorCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi85 – 939ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein complex binding Source: RGD
  • protein serine/threonine kinase activity Source: UniProtKB
  • signal transducer activity Source: Ensembl

GO - Biological processi

  • G1/S transition of mitotic cell cycle Source: UniProtKB
  • long term synaptic depression Source: UniProtKB
  • long-term synaptic potentiation Source: UniProtKB
  • memory Source: UniProtKB
  • mitotic cell cycle checkpoint Source: UniProtKB
  • mitotic spindle organization Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of dendritic spine development Source: RGD
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: RGD
  • positive regulation of protein binding Source: RGD
  • protein phosphorylation Source: UniProtKB
  • Rap protein signal transduction Source: UniProtKB
  • Ras protein signal transduction Source: UniProtKB
  • regulation of centriole replication Source: UniProtKB
  • 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. 5301.
ReactomeiR-RNO-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.

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
Serine/threonine-protein kinase SNK
Serum-inducible kinase
Gene namesi
Name:Plk2
Synonyms:Snk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi620760. Plk2.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB
  • centrosome Source: UniProtKB
  • chromatin Source: Ensembl
  • dendrite Source: UniProtKB
  • intracellular Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081K → M: Loss of kinase activity. 2 Publications
Mutagenesisi202 – 2021D → A: Loss of kinase activity. 1 Publication
Mutagenesisi236 – 2361T → E: Mimicks phosphorylation state, leading to increased activity. 2 Publications
Mutagenesisi504 – 5041W → A: Abolishes interaction with SIPA1L1. 2 Publications
Mutagenesisi504 – 5041W → F: Does not affect interaction with NSF and ability to dissociate NSF from GRIA2. 2 Publications

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 682682Serine/threonine-protein kinase PLK2PRO_0000086563Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei236 – 2361Phosphothreonine1 Publication

Post-translational modificationi

Catalytic activity is enhanced by phosphorylation of Thr-236.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9R012.
PRIDEiQ9R012.

PTM databases

iPTMnetiQ9R012.
PhosphoSiteiQ9R012.

Expressioni

Gene expression databases

GenevisibleiQ9R012. RN.

Interactioni

Subunit structurei

Interacts with CIB1 (By similarity). Interacts with NSF; causing NSF dissociation from GRIA2.By similarity2 Publications

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi249816. 5 interactions.
IntActiQ9R012. 1 interaction.
MINTiMINT-87366.
STRINGi10116.ENSRNOP00000016768.

Structurei

3D structure databases

ProteinModelPortaliQ9R012.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 331253Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini507 – 57064POLO box 1PROSITE-ProRule annotationAdd
BLAST
Domaini603 – 67472POLO box 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi54 – 596Poly-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

eggNOGiKOG0575. Eukaryota.
ENOG410XQBP. LUCA.
GeneTreeiENSGT00530000062954.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiQ9R012.
KOiK08861.
OMAiNGTHMSL.
OrthoDBiEOG78M01K.
PhylomeDBiQ9R012.
TreeFamiTF101089.

Family and domain databases

Gene3Di3.30.1120.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
IPR000959. POLO_box_duplicated_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.

Q9R012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELLRTITYQ PAAGTKMCEQ ALGKACGGDS KKKRPQQPSE DGQSQAQVTP
60 70 80 90 100
AAPHHHHHHS HSGPEISRII VDPTTGKRYC RGKVLGKGGF AKCYEMTDLT
110 120 130 140 150
NNKVYAAKII PHSRVAKPHQ REKIDKEIEL HRILHHKHVV QFYHYFEDKE
160 170 180 190 200
NIYILLEYCS RRSMAHILKA RKVLTEPEVR YYLRQIVSGL KYLHEQEILH
210 220 230 240 250
RDLKLGNFFI NEAMELKVGD FGLAARLEPL EHRRRTICGT PNYLSPEVLN
260 270 280 290 300
KQGHGCESDI WALGCVMYTM LLGRPPFETT NLKETYRCIR EARYTMPSSL
310 320 330 340 350
LAPAKHLIAS MLSKNPEDRP SLDDIIRHDF FLQGFTPDRL SSSCCHTVPD
360 370 380 390 400
FHLSSPAKNF FKKAAAALFG GKKDKARYND THNKVSKEDE DIYKLRHDLK
410 420 430 440 450
KTSITQQPSK HRTDEELQPP PTTFAKSGTS AVENKQQIGD AIRMIVRGTL
460 470 480 490 500
GSCSSSSECL EDSTMGSVAD TVARVLRGCL ENMPEADCIP KEQLSTSFQW
510 520 530 540 550
VTKWVDYSNK YGFGYQLSDH TVGVLFNNGA HMSLLPDKKT VHYYAELGQC
560 570 580 590 600
SVFPATDAPE QFISQVTVLK YFSHYMEENL MDGGDLPSVT DIRRPRLYLL
610 620 630 640 650
QWLKSDKALM MLFNDGTFQV NFYHDHTKII ICNQNEEYLL TYINEDRIST
660 670 680
TFRLTTLLMS GCSLELKHRM EYALNMLLQR CN
Length:682
Mass (Da):77,920
Last modified:May 1, 2000 - v1
Checksum:i58C50DEBDE83D5F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136583 mRNA. Translation: AAF08366.1.
BC070878 mRNA. Translation: AAH70878.1.
RefSeqiNP_114009.1. NM_031821.1.
UniGeneiRn.12100.

Genome annotation databases

EnsembliENSRNOT00000016768; ENSRNOP00000016768; ENSRNOG00000011951.
GeneIDi83722.
KEGGirno:83722.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136583 mRNA. Translation: AAF08366.1.
BC070878 mRNA. Translation: AAH70878.1.
RefSeqiNP_114009.1. NM_031821.1.
UniGeneiRn.12100.

3D structure databases

ProteinModelPortaliQ9R012.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249816. 5 interactions.
IntActiQ9R012. 1 interaction.
MINTiMINT-87366.
STRINGi10116.ENSRNOP00000016768.

PTM databases

iPTMnetiQ9R012.
PhosphoSiteiQ9R012.

Proteomic databases

PaxDbiQ9R012.
PRIDEiQ9R012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000016768; ENSRNOP00000016768; ENSRNOG00000011951.
GeneIDi83722.
KEGGirno:83722.

Organism-specific databases

CTDi10769.
RGDi620760. Plk2.

Phylogenomic databases

eggNOGiKOG0575. Eukaryota.
ENOG410XQBP. LUCA.
GeneTreeiENSGT00530000062954.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiQ9R012.
KOiK08861.
OMAiNGTHMSL.
OrthoDBiEOG78M01K.
PhylomeDBiQ9R012.
TreeFamiTF101089.

Enzyme and pathway databases

BRENDAi2.7.11.21. 5301.
ReactomeiR-RNO-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.

Miscellaneous databases

PROiQ9R012.

Gene expression databases

GenevisibleiQ9R012. RN.

Family and domain databases

Gene3Di3.30.1120.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
IPR000959. POLO_box_duplicated_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The polo-like protein kinases Fnk and Snk associate with a Ca(2+)- and integrin-binding protein and are regulated dynamically with synaptic plasticity."
    Kauselmann G., Weiler M., Wulff P., Jessberger S., Konietzko U., Scafidi J., Staubli U., Bereiter-Hahn J., Strebhardt K., Kuhl D.
    EMBO J. 18:5528-5539(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CIB1.
  2. "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: Lung.
  3. "Regulation of postsynaptic RapGAP SPAR by Polo-like kinase 2 and the SCFbeta-TRCP ubiquitin ligase in hippocampal neurons."
    Ang X.L., Seeburg D.P., Sheng M., Harper J.W.
    J. Biol. Chem. 283:29424-29432(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SIPA1L1, MUTAGENESIS OF ASP-202.
  4. "Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity."
    Seeburg D.P., Feliu-Mojer M., Gaiottino J., Pak D.T., Sheng M.
    Neuron 58:571-583(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SIPA1L1, MUTAGENESIS OF TRP-504.
  5. "Plk2 attachment to NSF induces homeostatic removal of GluA2 during chronic overexcitation."
    Evers D.M., Matta J.A., Hoe H.S., Zarkowsky D., Lee S.H., Isaac J.T., Pak D.T.
    Nat. Neurosci. 13:1199-1207(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NSF, PHOSPHORYLATION AT THR-236, MUTAGENESIS OF LYS-108; THR-236 AND TRP-504.
  6. "Requirement for Plk2 in orchestrated ras and rap signaling, homeostatic structural plasticity, and memory."
    Lee K.J., Lee Y., Rozeboom A., Lee J.Y., Udagawa N., Hoe H.S., Pak D.T.
    Neuron 69:957-973(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-108 AND THR-236.

Entry informationi

Entry nameiPLK2_RAT
AccessioniPrimary (citable) accession number: Q9R012
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.