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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)DescriptionActionsGraphical viewLength
Binding sitei108ATP1
Active sitei202Proton acceptorCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi85 – 93ATPPROSITE-ProRule annotation9

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
  • peptidyl-serine phosphorylation Source: Ensembl
  • positive regulation of autophagy Source: Ensembl
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi108K → M: Loss of kinase activity. 2 Publications1
Mutagenesisi202D → A: Loss of kinase activity. 1 Publication1
Mutagenesisi236T → E: Mimicks phosphorylation state, leading to increased activity. 2 Publications1
Mutagenesisi504W → A: Abolishes interaction with SIPA1L1. 2 Publications1
Mutagenesisi504W → F: Does not affect interaction with NSF and ability to dissociate NSF from GRIA2. 2 Publications1

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000865631 – 682Serine/threonine-protein kinase PLK2Add BLAST682

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei236Phosphothreonine1 Publication1

Post-translational modificationi

Catalytic activity is enhanced by phosphorylation of Thr-236.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9R012.
PRIDEiQ9R012.

PTM databases

iPTMnetiQ9R012.
PhosphoSitePlusiQ9R012.

Expressioni

Gene expression databases

BgeeiENSRNOG00000011951.
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 interactors.
IntActiQ9R012. 1 interactor.
MINTiMINT-87366.
STRINGi10116.ENSRNOP00000016768.

Structurei

3D structure databases

ProteinModelPortaliQ9R012.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini79 – 331Protein kinasePROSITE-ProRule annotationAdd BLAST253
Domaini507 – 570POLO box 1PROSITE-ProRule annotationAdd BLAST64
Domaini603 – 674POLO box 2PROSITE-ProRule annotationAdd BLAST72

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi54 – 59Poly-His6

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.
OrthoDBiEOG091G0D89.
PhylomeDBiQ9R012.
TreeFamiTF101089.

Family and domain databases

CDDicd13118. POLO_box_1. 1 hit.
cd13117. POLO_box_2. 1 hit.
Gene3Di3.30.1120.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
IPR033701. POLO_box_1.
IPR033695. POLO_box_2.
IPR000959. POLO_box_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 interactors.
IntActiQ9R012. 1 interactor.
MINTiMINT-87366.
STRINGi10116.ENSRNOP00000016768.

PTM databases

iPTMnetiQ9R012.
PhosphoSitePlusiQ9R012.

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.
OrthoDBiEOG091G0D89.
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

BgeeiENSRNOG00000011951.
GenevisibleiQ9R012. RN.

Family and domain databases

CDDicd13118. POLO_box_1. 1 hit.
cd13117. POLO_box_2. 1 hit.
Gene3Di3.30.1120.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
IPR033701. POLO_box_1.
IPR033695. POLO_box_2.
IPR000959. POLO_box_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...

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: November 2, 2016
This is version 122 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.