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Protein

Serine/threonine-protein kinase PLK3

Gene

Plk3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1 (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911ATPPROSITE-ProRule annotation
Active sitei185 – 1851Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi68 – 769ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • p53 binding Source: UniProtKB
  • protein kinase activity Source: RGD
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PLK3 (EC:2.7.11.21)
Alternative name(s):
Cytokine-inducible serine/threonine-protein kinase
FGF-inducible kinase
Polo-like kinase 3
Short name:
PLK-3
Gene namesi
Name:Plk3
Synonyms:Cnk, Fnk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi62039. Plk3.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • dendrite Source: RGD
  • Golgi stack Source: UniProtKB
  • neuronal cell body Source: RGD
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 647647Serine/threonine-protein kinase PLK3PRO_0000414709Add
BLAST

Post-translational modificationi

Phosphorylated in an ATM-dependent manner following DNA damage. Phosphorylated as cells enter mitosis and dephosphorylated as cells exit mitosis (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9R011.
PRIDEiQ9R011.

PTM databases

PhosphoSiteiQ9R011.

Expressioni

Tissue specificityi

Constitutively expressed in post-mitotic neurons.1 Publication

Inductioni

By the intense activity associated with seizures.1 Publication

Gene expression databases

GenevisibleiQ9R011. RN.

Interactioni

Subunit structurei

Interacts with GOLGB1 (By similarity). Interacts (via the POLO-box domain) with CIB1; leading to inhibit PLK3 kinase activity.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248673. 1 interaction.
STRINGi10116.ENSRNOP00000025197.

Structurei

3D structure databases

ProteinModelPortaliQ9R011.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 314253Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini471 – 53464POLO box 1PROSITE-ProRule annotationAdd
BLAST
Domaini568 – 63871POLO box 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK3 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them. The POLO box domains mediates localization to the centrosome (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.
InParanoidiQ9R011.
KOiK08862.
OMAiLCALRNC.
OrthoDBiEOG78M01K.
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.
IPR020658. Ser/Thr_kinase_Plk3.
[Graphical view]
PANTHERiPTHR24345:SF42. PTHR24345:SF42. 1 hit.
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.

Q9R011-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPAAGFLSP RPFPRAAAPS SPPAGPGPPA SASPRSEPGV LAGPQTPDAS
60 70 80 90 100
RLITDPRSGR TYIKGRLLGK GGFARCYEAT DTETSIAYAV KVIPQSRVAK
110 120 130 140 150
PHQREKIINE IELHRDLQHR HIVRFSHHFE DADNIYIFLE LCSRKSLAHI
160 170 180 190 200
WKARHTLLEP EVRYYLRQIL SGLKYLHQRG ILHRDLKLGN FFITDNMELK
210 220 230 240 250
VGDFGLAARL EPPEQRKKTI CGTPNYVAPE VLLRQGHGPE ADVWSLGCVM
260 270 280 290 300
YTLLCGSPPF ETADLKETYR CIKQVHYTLP ASLSLPARQL LAAILRASPR
310 320 330 340 350
DRPSIEQILR HDFFTKGYTP DRLPVSSCVT VPDLTPPNPA RSLFAKVTKS
360 370 380 390 400
LFGRRKSKNK NHSEEQDNVS CLVSGLMRTS IGHPDVRPEA PAASALAPVS
410 420 430 440 450
LVETAAEDSS PRGTLASSGD GFEEGLTVTT VVESALCALR NCVAFMPPAE
460 470 480 490 500
QNPAPLAQPE PLVWVSKWVD YSNKFGFGYQ LSSRRVAVLF NDGTHMALSA
510 520 530 540 550
NRKTVHYNPT STKHFSFSVG SVPRALQPQL GILRYFASYM EQHLMKGGDL
560 570 580 590 600
PSVEEVEVPA PPLLLQWVKT DQALLMLFSD GTVQVNFYGD HTKLILSGWE
610 620 630 640
PLLVTFVARN RSACTYLASH LRQLGCSPDL RQRLRYALRL LRDRSPA
Length:647
Mass (Da):71,768
Last modified:December 14, 2011 - v2
Checksum:i44FAFD446E5F9999
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136584 mRNA. Translation: AAF08367.1.
RefSeqiNP_071523.1. NM_022187.1.
UniGeneiRn.9284.

Genome annotation databases

EnsembliENSRNOT00000025197; ENSRNOP00000025197; ENSRNOG00000018484.
GeneIDi58936.
KEGGirno:58936.
UCSCiRGD:62039. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136584 mRNA. Translation: AAF08367.1.
RefSeqiNP_071523.1. NM_022187.1.
UniGeneiRn.9284.

3D structure databases

ProteinModelPortaliQ9R011.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248673. 1 interaction.
STRINGi10116.ENSRNOP00000025197.

PTM databases

PhosphoSiteiQ9R011.

Proteomic databases

PaxDbiQ9R011.
PRIDEiQ9R011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025197; ENSRNOP00000025197; ENSRNOG00000018484.
GeneIDi58936.
KEGGirno:58936.
UCSCiRGD:62039. rat.

Organism-specific databases

CTDi1263.
RGDi62039. Plk3.

Phylogenomic databases

eggNOGiKOG0575. Eukaryota.
ENOG410XQBP. LUCA.
GeneTreeiENSGT00530000062954.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiQ9R011.
KOiK08862.
OMAiLCALRNC.
OrthoDBiEOG78M01K.
TreeFamiTF101089.

Miscellaneous databases

NextBioi611513.
PROiQ9R011.

Gene expression databases

GenevisibleiQ9R011. 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.
IPR020658. Ser/Thr_kinase_Plk3.
[Graphical view]
PANTHERiPTHR24345:SF42. PTHR24345:SF42. 1 hit.
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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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], INTERACTION WITH CIB1, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPLK3_RAT
AccessioniPrimary (citable) accession number: Q9R011
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: December 14, 2011
Last modified: May 11, 2016
This is version 121 of the entry and version 2 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.