Serine/threonine-protein kinase PLK1 - Xenopus laevis (African clawed frog)

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P70032 (PLK1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	598 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle. 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 process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Nucleus
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological_process	G2 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 cytokinesis 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 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
Cellular_component	centrosome 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 midzone Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule binding Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay PubMed 16600872 Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 598

598

Serine/threonine-protein kinase PLK1

PRO_0000086559

Regions

Domain

44 – 296

253

Protein kinase

Domain

411 – 474

POLO box 1

Domain

509 – 578

POLO box 2

Nucleotide binding

50 – 58

ATP By similarity

Nucleotide binding

169 – 172

ATP By similarity

Region

185 – 212

Activation loop By similarity

Region

487 – 501

Linker By similarity

Region

532 – 534

Important for interaction with phosphorylated proteins By similarity

Motif

328 – 331

D-box that targets the protein for proteasomal degradation in anaphase By similarity

Sites

Active site

167

Proton acceptor By similarity

Binding site

ATP By similarity

Binding site

122

ATP; via carbonyl oxygen By similarity

Binding site

185

ATP By similarity

Amino acid modifications

Modified residue

Phosphothreonine; by PKA; in vitro Ref.5

Modified residue

Phosphoserine Probable

Modified residue

Phosphoserine Probable

Modified residue

201

Phosphothreonine; by PKA Ref.4 Ref.5

Modified residue

260

Phosphoserine; by autocatalysis Ref.5

Modified residue

326

Phosphoserine; by autocatalysis Ref.5

Modified residue

340

Phosphoserine; by CDK1 Ref.5

Experimental info

Mutagenesis

128

S → A: No effect on activity. Ref.4 Ref.5

Mutagenesis

128

S → D: Increases activity. Ref.4 Ref.5

Mutagenesis

140

T → D: No effect on activity. Ref.4

Mutagenesis

172

N → A: Abolishes activity. Ref.3 Ref.5

Mutagenesis

201

T → A: Abolishes activity. Ref.4 Ref.5

Mutagenesis

201

T → D: Increases activity. Ref.4 Ref.5

Mutagenesis

201

T → V: Abolishes activity. Ref.4 Ref.5

Mutagenesis

205

T → D: No effect on activity. Ref.4

Mutagenesis

227

S → D: No effect on activity. Ref.4

Mutagenesis

340

S → A: No effect on activity. Ref.5

Mutagenesis

340

S → D: No effect on activity. Ref.5

Sequence conflict

348

A → V in AAH46839. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P70032 [UniParc].

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

598

68,212

        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' referencesShow '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, 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.
RefSeq	NP_001080788.1. NM_001087319.1.
UniGene	Xl.28141.
3D structure databases
ProteinModelPortal	P70032.
SMR	P70032. Positions 29-321, 365-588.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42603N.
IntAct	P70032. 1 interaction.
MINT	MINT-1532390.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	380481.
KEGG	xla:380481.
Organism-specific databases
CTD	5347.
Xenbase	XB-GENE-941545. plk1.
Phylogenomic databases
HOVERGEN	HBG001843.
KO	K06631.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000959. POLO_box_duplicated_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF00659. POLO_box. 2 hits. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50078. POLO_BOX. 2 hits. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P70032.
ChEMBL	CHEMBL4519.

Entry information

Entry name

PLK1_XENLA

Accession

Primary (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:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents