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P70032 (PLK1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PLK1

EC=2.7.11.21
Alternative name(s):
Plx1
Polo-like kinase 1
Short name=PLK-1
Gene names
Name:plk1
Synonyms:plx1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates cdc25, pkmyt1/myt1, stag2/sa2, tpx2. Plays multiple essential roles during mitosis. Phosphorylates the N-terminal domain of cdc25, which leads to cyclin b-cdc2 activation and mitotic entry. Also required for organization of bipolar spindles, and for exit from mitosis. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating stag2/sa2. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by phosphorylation of Thr-201. Ref.4

Subunit structure

Interacts with plk1 and kif2a. Ref.9 Ref.10

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Midbody By similarity. Note: Localized at centrosomes at prophase, spindles at metaphase, and at the midbody during cytokinesis. Ref.4

Induction

By growth-stimulating agents By similarity. Ref.4

Domain

The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. plk1 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them By similarity.

Post-translational modification

Activated by phosphorylation on Thr-201 during M phase. Phosphorylated by stk10, leading to activation during oocyte maturation. Ref.3 Ref.4 Ref.5

Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) in anaphase and following DNA damage, leading to its degradation by the proteasome. Protein levels are down-regulated by proteasomal degradation in anaphase By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 2 POLO box domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
Gene Ontology (GO)
   Biological_processG2 DNA damage checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

G2/M transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

activation of mitotic anaphase-promoting complex activity

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome organization

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule bundle formation

Inferred from sequence or structural similarity. Source: UniProtKB

mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

oocyte maturation

Inferred from direct assay Ref.3. Source: UniProtKB

protein localization to chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

kinetochore

Inferred from sequence or structural similarity. Source: UniProtKB

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

spindle

Inferred from sequence or structural similarity. Source: UniProtKB

spindle midzone

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.3. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay PubMed 16600872Ref.3. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

fbxo5-aQ90Z802EBI-3511304,EBI-7161111
mcm7-aQ918763EBI-3511304,EBI-876852

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 598598Serine/threonine-protein kinase PLK1
PRO_0000086559

Regions

Domain44 – 296253Protein kinase
Domain411 – 47464POLO box 1
Domain509 – 57870POLO box 2
Nucleotide binding50 – 589ATP By similarity
Nucleotide binding169 – 1724ATP By similarity
Region185 – 21228Activation loop By similarity
Region487 – 50115Linker By similarity
Region532 – 5343Important for interaction with phosphorylated proteins By similarity
Motif328 – 3314D-box that targets the protein for proteasomal degradation in anaphase By similarity

Sites

Active site1671Proton acceptor By similarity
Binding site731ATP By similarity
Binding site1221ATP; via carbonyl oxygen By similarity
Binding site1851ATP By similarity

Amino acid modifications

Modified residue101Phosphothreonine; by PKA; in vitro Ref.5
Modified residue251Phosphoserine Probable
Modified residue261Phosphoserine Probable
Modified residue2011Phosphothreonine; by PKA Ref.4 Ref.5
Modified residue2601Phosphoserine; by autocatalysis Ref.5
Modified residue3261Phosphoserine; by autocatalysis Ref.5
Modified residue3401Phosphoserine; by CDK1 Ref.5

Experimental info

Mutagenesis1281S → A: No effect on activity. Ref.4 Ref.5
Mutagenesis1281S → D: Increases activity. Ref.4 Ref.5
Mutagenesis1401T → D: No effect on activity. Ref.4
Mutagenesis1721N → A: Abolishes activity. Ref.3 Ref.5
Mutagenesis2011T → A: Abolishes activity. Ref.4 Ref.5
Mutagenesis2011T → D: Increases activity. Ref.4 Ref.5
Mutagenesis2011T → V: Abolishes activity. Ref.4 Ref.5
Mutagenesis2051T → D: No effect on activity. Ref.4
Mutagenesis2271S → D: No effect on activity. Ref.4
Mutagenesis3401S → A: No effect on activity. Ref.5
Mutagenesis3401S → D: No effect on activity. Ref.5
Sequence conflict3481A → V in AAH46839. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P70032 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 2467195911F225E6

FASTA59868,212
        10         20         30         40         50         60 
MAQVAGKKLT VAPEAAKPPG IPGSSSAVKE IPEILVDPRT RRRYLRGRFL GKGGFAKCYE 

        70         80         90        100        110        120 
ITDLESREVF AGKIVPKTML LKPHQKDKMT MEIAIQRSLD HRHVVGFHGF FEDNDFVYVV 

       130        140        150        160        170        180 
LELCRRRSLL ELHKRRKAVT EPEARYYLKQ TISGCQYLHS NRVIHRDLKL GNLFLNDEME 

       190        200        210        220        230        240 
VKIGDFGLAT KVEYDGERKK TLCGTPNYIA PEVLGKKGHS FEVDIWSIGC IMYTLLVGKP 

       250        260        270        280        290        300 
PFETSCLKET YMRIKKNEYS IPKHINPVAA ALIQKMLRSD PTSRPTIDDL LNDEFFTSGY 

       310        320        330        340        350        360 
IPSRLPTTCL TVPPRFSIAP STIDQSLRKP LTAINKGQDS PLVEKQVAPA KEEEMQQPEF 

       370        380        390        400        410        420 
TEPADCYLSE MLQQLTCLNA VKPSERALIR QEEAEDPASI PIFWISKWVD YSDKYGLGYQ 

       430        440        450        460        470        480 
LCDNSVGVLF NDSTRLIMYN DGDSLQYIER NNTESYLNVR SYPTTLTKKI TLLKYFRNYM 

       490        500        510        520        530        540 
SEHLLKAGAN TTPREGDELA RLPFLRTWFR TRSAIILHLS NGTVQINFFQ DHTKIILCPL 

       550        560        570        580        590 
MAAVSYIDEK REFRTYKLSL IQEFGCCKEL ASRLRYARTM VEKLQSSKSA VAHVKASA 

« Hide

References

« Hide 'large scale' references
[1]"Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts."
Kumagai A., Dunphy W.G.
Science 273:1377-1380(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Oocyte.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[3]"Purification and cloning of a protein kinase that phosphorylates and activates the polo-like kinase Plx1."
Qian Y.W., Erikson E., Maller J.L.
Science 282:1701-1704(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY STK10, FUNCTION, MUTAGENESIS OF ASN-172.
[4]"Mitotic effects of a constitutively active mutant of the Xenopus polo-like kinase Plx1."
Qian Y.W., Erikson E., Maller J.L.
Mol. Cell. Biol. 19:8625-8632(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-201, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-128; THR-140; THR-201; THR-205 AND SER-227.
[5]"Cell cycle-regulated phosphorylation of the Xenopus polo-like kinase Plx1."
Kelm O., Wind M., Lehmann W.D., Nigg E.A.
J. Biol. Chem. 277:25247-25256(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-10; SER-25; SER-26; THR-201; SER-260; SER-326 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-128; ASN-172; THR-201 AND SER-340.
[6]"The dissociation of cohesin from chromosomes in prophase is regulated by Polo-like kinase."
Sumara I., Vorlaufer E., Stukenberg P.T., Kelm O., Redemann N., Nigg E.A., Peters J.-M.
Mol. Cell 9:515-525(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF STAG2.
[7]"Polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores."
Ahonen L.J., Kallio M.J., Daum J.R., Bolton M., Manke I.A., Yaffe M.B., Stukenberg P.T., Gorbsky G.J.
Curr. Biol. 15:1078-1089(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The Polo-like kinase Plx1 interacts with and inhibits Myt1 after fertilization of Xenopus eggs."
Inoue D., Sagata N.
EMBO J. 24:1057-1067(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PKMYT1.
[9]"Phosphorylation of TPX2 by Plx1 enhances activation of Aurora A."
Eckerdt F., Pascreau G., Phistry M., Lewellyn A.L., DePaoli-Roach A.A., Maller J.L.
Cell Cycle 8:2413-2419(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TPX2, FUNCTION.
[10]"Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a."
Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.
J. Cell Sci. 122:1334-1341(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KIF2A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U58205 mRNA. Translation: AAC60017.1.
BC046839 mRNA. Translation: AAH46839.1.
RefSeqNP_001080788.1. NM_001087319.1.
UniGeneXl.28141.

3D structure databases

ProteinModelPortalP70032.
SMRP70032. Positions 29-321, 365-588.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid98723. 5 interactions.
DIPDIP-42603N.
IntActP70032. 7 interactions.
MINTMINT-1532390.

Chemistry

BindingDBP70032.
ChEMBLCHEMBL4519.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID380481.
KEGGxla:380481.

Organism-specific databases

CTD5347.
XenbaseXB-GENE-941545. plk1.

Phylogenomic databases

HOVERGENHBG001843.
KOK06631.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000959. POLO_box_duplicated_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLK1_XENLA
AccessionPrimary (citable) accession number: P70032
Secondary accession number(s): Q7ZWQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families