Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein kinase PLK1

Gene

plk1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei73ATPPROSITE-ProRule annotation1
Binding sitei122ATP; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei167Proton acceptorPROSITE-ProRule annotation1
Binding sitei185ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi50 – 58ATPPROSITE-ProRule annotation9
Nucleotide bindingi169 – 172ATPPROSITE-ProRule annotation4

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Mitosis
LigandATP-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: localization at the centrosome starts at the G1/S transition (By similarity). Localized at centrosomes at prophase, spindles at metaphase, and at the midbody during cytokinesis. Localization to the centrosome is required for S phase progression (By similarity).By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi128S → A: No effect on activity. 2 Publications1
Mutagenesisi128S → D: Increases activity. 2 Publications1
Mutagenesisi140T → D: No effect on activity. 1 Publication1
Mutagenesisi172N → A: Abolishes activity. 2 Publications1
Mutagenesisi201T → A: Abolishes activity. 2 Publications1
Mutagenesisi201T → D: Increases activity. 2 Publications1
Mutagenesisi201T → V: Abolishes activity. 2 Publications1
Mutagenesisi205T → D: No effect on activity. 1 Publication1
Mutagenesisi227S → D: No effect on activity. 1 Publication1
Mutagenesisi340S → A: No effect on activity. 1 Publication1
Mutagenesisi340S → D: No effect on activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4519.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000865591 – 598Serine/threonine-protein kinase PLK1Add BLAST598

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10Phosphothreonine; by PKA; in vitro1 Publication1
Modified residuei25Phosphoserine1 Publication1
Modified residuei26Phosphoserine1 Publication1
Modified residuei201Phosphothreonine; by PKA2 Publications1
Modified residuei260Phosphoserine; by autocatalysis1 Publication1
Modified residuei326Phosphoserine; by autocatalysis1 Publication1
Modified residuei340Phosphoserine; by CDK11 Publication1

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

PTM databases

iPTMnetiP70032.

Expressioni

Inductioni

By growth-stimulating agents.By similarity

Interactioni

Subunit structurei

Interacts with plk1 and kif2a.2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi98723. 8 interactors.
DIPiDIP-42603N.
IntActiP70032. 9 interactors.
MINTiMINT-1532390.

Chemistry databases

BindingDBiP70032.

Structurei

3D structure databases

ProteinModelPortaliP70032.
SMRiP70032.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 296Protein kinasePROSITE-ProRule annotationAdd BLAST253
Domaini411 – 474POLO box 1PROSITE-ProRule annotationAdd BLAST64
Domaini509 – 578POLO box 2PROSITE-ProRule annotationAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni185 – 212Activation loopBy similarityAdd BLAST28
Regioni487 – 501LinkerBy similarityAdd BLAST15
Regioni532 – 534Important for interaction with phosphorylated proteinsBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi328 – 331D-box that targets the protein for proteasomal degradation in anaphaseBy similarity4

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

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG001843.
KOiK06631.

Family and domain databases

CDDicd13118. POLO_box_1. 1 hit.
cd13117. POLO_box_2. 1 hit.
cd14187. STKc_PLK1. 1 hit.
Gene3Di3.30.1120.30. 2 hits.
InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
IPR033702. PLK1_cat.
IPR033701. POLO_box_1.
IPR033695. POLO_box_2.
IPR000959. POLO_box_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
SMARTiView protein in SMART
SM00220. S_TKc. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti348A → V in AAH46839 (Ref. 2) Curated1

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.

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.

Entry informationi

Entry nameiPLK1_XENLA
AccessioniPrimary (citable) accession number: P70032
Secondary accession number(s): Q7ZWQ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: February 1, 1997
Last modified: June 7, 2017
This is version 123 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families