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P70032

- PLK1_XENLA

UniProt

P70032 - PLK1_XENLA

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
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    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 binding Source: IntAct
    4. protein kinase binding Source: UniProtKB
    5. 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

    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

    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 vitro2 Publications
    Modified residuei25 – 251Phosphoserine2 Publications
    Modified residuei26 – 261Phosphoserine2 Publications
    Modified residuei201 – 2011Phosphothreonine; by PKA3 Publications
    Modified residuei260 – 2601Phosphoserine; by autocatalysis2 Publications
    Modified residuei326 – 3261Phosphoserine; by autocatalysis2 Publications
    Modified residuei340 – 3401Phosphoserine; by CDK12 Publications

    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_dom.
    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

    MAQVAGKKLT VAPEAAKPPG IPGSSSAVKE IPEILVDPRT RRRYLRGRFL    50
    GKGGFAKCYE ITDLESREVF AGKIVPKTML LKPHQKDKMT MEIAIQRSLD 100
    HRHVVGFHGF FEDNDFVYVV LELCRRRSLL ELHKRRKAVT EPEARYYLKQ 150
    TISGCQYLHS NRVIHRDLKL GNLFLNDEME VKIGDFGLAT KVEYDGERKK 200
    TLCGTPNYIA PEVLGKKGHS FEVDIWSIGC IMYTLLVGKP PFETSCLKET 250
    YMRIKKNEYS IPKHINPVAA ALIQKMLRSD PTSRPTIDDL LNDEFFTSGY 300
    IPSRLPTTCL TVPPRFSIAP STIDQSLRKP LTAINKGQDS PLVEKQVAPA 350
    KEEEMQQPEF TEPADCYLSE MLQQLTCLNA VKPSERALIR QEEAEDPASI 400
    PIFWISKWVD YSDKYGLGYQ LCDNSVGVLF NDSTRLIMYN DGDSLQYIER 450
    NNTESYLNVR SYPTTLTKKI TLLKYFRNYM SEHLLKAGAN TTPREGDELA 500
    RLPFLRTWFR TRSAIILHLS NGTVQINFFQ DHTKIILCPL MAAVSYIDEK 550
    REFRTYKLSL IQEFGCCKEL ASRLRYARTM VEKLQSSKSA VAHVKASA 598
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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_dom.
    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

    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 1, 2014
    This is version 107 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