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P70032

- PLK1_XENLA

UniProt

P70032 - PLK1_XENLA

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Protein

Serine/threonine-protein kinase PLK1

Gene

plk1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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/sa2.9 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by phosphorylation of Thr-201.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731ATPPROSITE-ProRule annotation
Binding sitei122 – 1221ATP; via carbonyl oxygenPROSITE-ProRule annotation
Active sitei167 – 1671Proton acceptorPROSITE-ProRule annotation
Binding sitei185 – 1851ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi50 – 589ATPPROSITE-ProRule annotation
Nucleotide bindingi169 – 1724ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. microtubule binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of mitotic anaphase-promoting complex activity Source: UniProtKB
  2. centrosome organization Source: UniProtKB
  3. G2/M transition of mitotic cell cycle Source: UniProtKB
  4. G2 DNA damage checkpoint Source: UniProtKB
  5. microtubule bundle formation Source: UniProtKB
  6. mitotic cytokinesis Source: UniProtKB
  7. mitotic nuclear division Source: UniProtKB
  8. negative regulation of apoptotic process Source: UniProtKB
  9. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  10. oocyte maturation Source: UniProtKB
  11. protein localization to chromatin Source: UniProtKB
  12. protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:plk1
Synonyms:plx1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-941545. plk1.

Subcellular locationi

Nucleus 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication. Midbody By similarity
Note: Localized at centrosomes at prophase, spindles at metaphase, and at the midbody during cytokinesis.

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. kinetochore Source: UniProtKB
  4. midbody Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. spindle Source: UniProtKB
  7. spindle midzone Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi128 – 1281S → A: No effect on activity. 2 Publications
Mutagenesisi128 – 1281S → D: Increases activity. 2 Publications
Mutagenesisi140 – 1401T → D: No effect on activity. 1 Publication
Mutagenesisi172 – 1721N → A: Abolishes activity. 2 Publications
Mutagenesisi201 – 2011T → A: Abolishes activity. 2 Publications
Mutagenesisi201 – 2011T → D: Increases activity. 2 Publications
Mutagenesisi201 – 2011T → V: Abolishes activity. 2 Publications
Mutagenesisi205 – 2051T → D: No effect on activity. 1 Publication
Mutagenesisi227 – 2271S → D: No effect on activity. 1 Publication
Mutagenesisi340 – 3401S → A: No effect on activity. 1 Publication
Mutagenesisi340 – 3401S → D: No effect on activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 598598Serine/threonine-protein kinase PLK1PRO_0000086559Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphothreonine; by PKA; in vitro1 Publication
Modified residuei25 – 251Phosphoserine1 Publication
Modified residuei26 – 261Phosphoserine1 Publication
Modified residuei201 – 2011Phosphothreonine; by PKA2 Publications
Modified residuei260 – 2601Phosphoserine; by autocatalysis1 Publication
Modified residuei326 – 3261Phosphoserine; by autocatalysis1 Publication
Modified residuei340 – 3401Phosphoserine; by CDK11 Publication

Post-translational modificationi

Activated by phosphorylation on Thr-201 during M phase. Phosphorylated by stk10, leading to activation during oocyte maturation.3 Publications
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).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Expressioni

Inductioni

By growth-stimulating agents.By similarity

Interactioni

Subunit structurei

Interacts with plk1 and kif2a.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
fbxo5-aQ90Z802EBI-3511304,EBI-7161111
mcm7-aQ918763EBI-3511304,EBI-876852

Protein-protein interaction databases

BioGridi98723. 5 interactions.
DIPiDIP-42603N.
IntActiP70032. 7 interactions.
MINTiMINT-1532390.

Structurei

3D structure databases

ProteinModelPortaliP70032.
SMRiP70032. Positions 29-321, 365-588.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 296253Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini411 – 47464POLO box 1PROSITE-ProRule annotationAdd
BLAST
Domaini509 – 57870POLO box 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 21228Activation loopBy similarityAdd
BLAST
Regioni487 – 50115LinkerBy similarityAdd
BLAST
Regioni532 – 5343Important for interaction with phosphorylated proteinsBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi328 – 3314D-box that targets the protein for proteasomal degradation in anaphaseBy similarity

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 2 POLO box domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG001843.
KOiK06631.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000959. POLO_box_duplicated_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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.

P70032-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQVAGKKLT VAPEAAKPPG IPGSSSAVKE IPEILVDPRT RRRYLRGRFL
60 70 80 90 100
GKGGFAKCYE ITDLESREVF AGKIVPKTML LKPHQKDKMT MEIAIQRSLD
110 120 130 140 150
HRHVVGFHGF FEDNDFVYVV LELCRRRSLL ELHKRRKAVT EPEARYYLKQ
160 170 180 190 200
TISGCQYLHS NRVIHRDLKL GNLFLNDEME VKIGDFGLAT KVEYDGERKK
210 220 230 240 250
TLCGTPNYIA PEVLGKKGHS FEVDIWSIGC IMYTLLVGKP PFETSCLKET
260 270 280 290 300
YMRIKKNEYS IPKHINPVAA ALIQKMLRSD PTSRPTIDDL LNDEFFTSGY
310 320 330 340 350
IPSRLPTTCL TVPPRFSIAP STIDQSLRKP LTAINKGQDS PLVEKQVAPA
360 370 380 390 400
KEEEMQQPEF TEPADCYLSE MLQQLTCLNA VKPSERALIR QEEAEDPASI
410 420 430 440 450
PIFWISKWVD YSDKYGLGYQ LCDNSVGVLF NDSTRLIMYN DGDSLQYIER
460 470 480 490 500
NNTESYLNVR SYPTTLTKKI TLLKYFRNYM SEHLLKAGAN TTPREGDELA
510 520 530 540 550
RLPFLRTWFR TRSAIILHLS NGTVQINFFQ DHTKIILCPL MAAVSYIDEK
560 570 580 590
REFRTYKLSL IQEFGCCKEL ASRLRYARTM VEKLQSSKSA VAHVKASA
Length:598
Mass (Da):68,212
Last modified:February 1, 1997 - v1
Checksum:i2467195911F225E6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti348 – 3481A → V in AAH46839. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58205 mRNA. Translation: AAC60017.1.
BC046839 mRNA. Translation: AAH46839.1.
RefSeqiNP_001080788.1. NM_001087319.1.
UniGeneiXl.28141.

Genome annotation databases

GeneIDi380481.
KEGGixla:380481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58205 mRNA. Translation: AAC60017.1 .
BC046839 mRNA. Translation: AAH46839.1 .
RefSeqi NP_001080788.1. NM_001087319.1.
UniGenei Xl.28141.

3D structure databases

ProteinModelPortali P70032.
SMRi P70032. Positions 29-321, 365-588.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 98723. 5 interactions.
DIPi DIP-42603N.
IntActi P70032. 7 interactions.
MINTi MINT-1532390.

Chemistry

BindingDBi P70032.
ChEMBLi CHEMBL4519.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 380481.
KEGGi xla:380481.

Organism-specific databases

CTDi 5347.
Xenbasei XB-GENE-941545. plk1.

Phylogenomic databases

HOVERGENi HBG001843.
KOi K06631.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000959. POLO_box_duplicated_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiPLK1_XENLA
AccessioniPrimary (citable) accession number: P70032
Secondary accession number(s): Q7ZWQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3