EKS-HOS-00268
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00268
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
Other/PLK427.31.1E-12753305253
StatusReviewed
Ensembl ProteinENSP00000300093
UniProt AccessionP53350; Q15153; Q99746;
Protein NameSerine/threonine-protein kinase PLK1
Protein Synonyms/Alias Polo-like kinase 1; PLK-1; Serine/threonine-protein kinase 13; STPK13;
Gene NamePLK1
Gene Synonyms/Alias PLK1; PLK;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000166851ENSP00000460266ENST00000570220
ENSG00000166851ENSP00000459688ENST00000567897
ENSG00000166851ENSP00000460084ENST00000568568
ENSG00000166851ENSP00000300093ENST00000300093
OrganismHomo sapiens
Functional DescriptionSerine/threonine-protein kinase that performs severalimportant 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 BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, MLF1IP, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, PLK1S1/KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGOL1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1 and WEE1. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating PLK1S1/KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, MLF1IP, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, MLF1IP, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatide cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGOL1: required for spindle pole localization of isoform 3 of SGOL1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73- mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis.
Protein Length603
Protein Sequence
(FASTA)
MSAAVTAGKL ARAPADPGKA GVPGVAAPGA PAAAPPAKEI PEVLVDPRSR RRYVRGRFLG 60
KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQREKMSM EISIHRSLAH QHVVGFHGFF 120
EDNDFVFVVL ELCRRRSLLE LHKRRKALTE PEARYYLRQI VLGCQYLHRN RVIHRDLKLG 180
NLFLNEDLEV KIGDFGLATK VEYDGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI 240
MYTLLVGKPP FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTINELL 300
NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSNRKPL TVLNKGLENP LPERPREKEE 360
PVVRETGEVV DCHLSDMLQQ LHSVNASKPS ERGLVRQEEA EDPACIPIFW VSKWVDYSDK 420
YGLGYQLCDN SVGVLFNDST RLILYNDGDS LQYIERDGTE SYLTVSSHPN SLMKKITLLK 480
YFRNYMSEHL LKAGANITPR EGDELARLPY LRTWFRTRSA IILHLSNGSV QINFFQDHTK 540
LILCPLMAAV TYIDEKRDFR TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL 600
KAS 603
Nucleotide Sequence
(FASTA)
ATGAGTGCTG CAGTGACTGC AGGGAAGCTG GCACGGGCAC CGGCCGACCC TGGGAAAGCC 60
GGGGTCCCCG GAGTTGCAGC TCCCGGAGCT CCGGCGGCGG CTCCACCGGC GAAAGAGATC 120
CCGGAGGTCC TAGTGGACCC ACGCAGCCGG CGGCGCTATG TGCGGGGCCG CTTTTTGGGC 180
AAGGGCGGCT TTGCCAAGTG CTTCGAGATC TCGGACGCGG ACACCAAGGA GGTGTTCGCG 240
GGCAAGATTG TGCCTAAGTC TCTGCTGCTC AAGCCGCACC AGAGGGAGAA GATGTCCATG 300
GAAATATCCA TTCACCGCAG CCTCGCCCAC CAGCACGTCG TAGGATTCCA CGGCTTTTTC 360
GAGGACAACG ACTTCGTGTT CGTGGTGTTG GAGCTCTGCC GCCGGAGGTC TCTCCTGGAG 420
CTGCACAAGA GGAGGAAAGC CCTGACTGAG CCTGAGGCCC GATACTACCT ACGGCAAATT 480
GTGCTTGGCT GCCAGTACCT GCACCGAAAC CGAGTTATTC ATCGAGACCT CAAGCTGGGC 540
AACCTTTTCC TGAATGAAGA TCTGGAGGTG AAAATAGGGG ATTTTGGACT GGCAACCAAA 600
GTCGAATATG ACGGGGAGAG GAAGAAGACC CTGTGTGGGA CTCCTAATTA CATAGCTCCC 660
GAGGTGCTGA GCAAGAAAGG GCACAGTTTC GAGGTGGATG TGTGGTCCAT TGGGTGTATC 720
ATGTATACCT TGTTAGTGGG CAAACCACCT TTTGAGACTT CTTGCCTAAA AGAGACCTAC 780
CTCCGGATCA AGAAGAATGA ATACAGTATT CCCAAGCACA TCAACCCCGT GGCCGCCTCC 840
CTCATCCAGA AGATGCTTCA GACAGATCCC ACTGCCCGCC CAACCATTAA CGAGCTGCTT 900
AATGACGAGT TCTTTACTTC TGGCTATATC CCTGCCCGTC TCCCCATCAC CTGCCTGACC 960
ATTCCACCAA GGTTTTCGAT TGCTCCCAGC AGCCTGGACC CCAGCAACCG GAAGCCCCTC 1020
ACAGTCCTCA ATAAAGGCTT GGAGAACCCC CTGCCTGAGC GTCCCCGGGA AAAAGAAGAA 1080
CCAGTGGTTC GAGAGACAGG TGAGGTGGTC GACTGCCACC TCAGTGACAT GCTGCAGCAG 1140
CTGCACAGTG TCAATGCCTC CAAGCCCTCG GAGCGTGGGC TGGTCAGGCA AGAGGAGGCT 1200
GAGGATCCTG CCTGCATCCC CATCTTCTGG GTCAGCAAGT GGGTGGACTA TTCGGACAAG 1260
TACGGCCTTG GGTATCAGCT CTGTGATAAC AGCGTGGGGG TGCTCTTCAA TGACTCAACA 1320
CGCCTCATCC TCTACAATGA TGGTGACAGC CTGCAGTACA TAGAGCGTGA CGGCACTGAG 1380
TCCTACCTCA CCGTGAGTTC CCATCCCAAC TCCTTGATGA AGAAGATCAC CCTCCTTAAA 1440
TATTTCCGCA ATTACATGAG CGAGCACTTG CTGAAGGCAG GTGCCAACAT CACGCCGCGC 1500
GAAGGTGATG AGCTCGCCCG GCTGCCCTAC CTACGGACCT GGTTCCGCAC CCGCAGCGCC 1560
ATCATCCTGC ACCTCAGCAA CGGCAGCGTG CAGATCAACT TCTTCCAGGA TCACACCAAG 1620
CTCATCTTGT GCCCACTGAT GGCAGCCGTG ACCTACATCG ACGAGAAGCG GGACTTCCGC 1680
ACATACCGCC TGAGTCTCCT GGAGGAGTAC GGCTGCTGCA AGGAGCTGGC CAGCCGGCTC 1740
CGCTACGCCC GCACTATGGT GGACAAGCTG CTGAGCTCAC GCTCGGCCAG CAACCGTCTC 1800
AAGGCCTCCT AA 1812
Domain Profile
S: 1     yergkllGkGgfakcyelkdletkevfavkvvpksllakekqrekvekeieihrslkhkn  60
         y rg++lGkGgfakc+e++d++tkevfa k+vpksll k++qrek+++ei+ihrsl+h++
Q: 53    YVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQH  112
         89**********************************************************
S: 61    ivklyeffedkenvylvlelcsrrslaellkrrkaltepevryylrqivsglkylhekri  120
         +v ++ ffed+++v++vlelc+rrsl el+krrkaltepe+ryylrqiv g++ylh++r+
Q: 113   VVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRV  172
         ************************************************************
S: 121   lhrdlklgnlflneelevkigdfGlatrlekeeerkktlcGtPnyiaPevlskkghslev  180
         +hrdlklgnlflne+levkigdfGlat++e+++erkktlcGtPnyiaPevlskkghs+ev
Q: 173   IHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEV  232
         ************************************************************
S: 181   diWslGcilytllvGkPPfetkelketyekikkaeyslPsslskeaksliakllkkePee  240
         d+Ws+Gci+ytllvGkPPfet++lkety +ikk+eys+P+++++ a+sli+k+l+++P++
Q: 233   DVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTA  292
         ************************************************************
S: 241   rpsleevlkdefl  253
         rp+++e+l+def+
Q: 293   RPTINELLNDEFF  305
         ************8
Domain Sequence
(FASTA)
YVRGRFLGKG GFAKCFEISD ADTKEVFAGK IVPKSLLLKP HQREKMSMEI SIHRSLAHQH 60
VVGFHGFFED NDFVFVVLEL CRRRSLLELH KRRKALTEPE ARYYLRQIVL GCQYLHRNRV 120
IHRDLKLGNL FLNEDLEVKI GDFGLATKVE YDGERKKTLC GTPNYIAPEV LSKKGHSFEV 180
DVWSIGCIMY TLLVGKPPFE TSCLKETYLR IKKNEYSIPK HINPVAASLI QKMLQTDPTA 240
RPTINELLND EFF 253
Keyword3D-structure; ATP-binding; Cell cycle; Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Kinetochore; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase; Ubl conjugation.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Caenorhabditis elegans"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Ciona intestinalis"; ?>Ciona savignyi"; ?>Danio rerio"; ?>Drosophila melanogaster"; ?>Echinops telfairi"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Macropus eugenii"; ?>Meleagris gallopavo"; ?>Microcebus murinus"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Tupaia belangeri"; ?>Tursiops truncatus"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00244
EKS-ANC-00253
EKS-BOT-00261
EKS-CAE-00235
EKS-CAJ-00267
EKS-CAF-00268
EKS-CAP-00296
EKS-CII-00158
EKS-CIS-00035
EKS-DAR-00596
EKS-DRM-00134
EKS-ECT-00012
EKS-EQC-00256
EKS-FEC-00247
EKS-GAM-00161
EKS-GAG-00220
EKS-GAA-00322
EKS-GOG-00259
EKS-ICT-00246
EKS-LAC-00273
EKS-LOA-00271
EKS-MAM-00263
EKS-MAE-00014
EKS-MEG-00209
EKS-MIM-00017
EKS-MOD-00258
EKS-MUM-00291
EKS-MUP-00258
EKS-MYL-00262
EKS-ORN-00340
EKS-ORA-00231
EKS-ORC-00247
EKS-ORL-00317
EKS-OTG-00267
EKS-PAT-00248
EKS-PES-00234
EKS-POA-00254
EKS-RAN-00276
EKS-SAH-00247
EKS-TAG-00279
EKS-TAR-00335
EKS-TEN-00331
EKS-TUB-00014
EKS-TUT-00029
EKS-XET-00336
EKS-XIM-00332
Gene Ontology
GO:0005813; C:centrosome
GO:0000942; C:condensed nuclear chromosome outer kinetochore
GO:0005829; C:cytosol
GO:0030496; C:midbody
GO:0005654; C:nucleoplasm
GO:0005876; C:spindle microtubule
GO:0051233; C:spindle midzone
GO:0000922; C:spindle pole
GO:0005524; F:ATP binding
GO:0008017; F:microtubule binding
GO:0004674; F:protein serine/threonine kinase activity
GO:0007092; P:activation of mitotic anaphase-promoting complex activity
GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process
GO:0008283; P:cell proliferation
GO:0051297; P:centrosome organization
GO:0000910; P:cytokinesis
GO:0031572; P:G2/M transition DNA damage checkpoint
GO:0000086; P:G2/M transition of mitotic cell cycle
GO:0001578; P:microtubule bundle formation
GO:0007091; P:mitotic metaphase/anaphase transition
GO:0000236; P:mitotic prometaphase
GO:0000088; P:mitotic prophase
GO:0043066; P:negative regulation of apoptotic process
GO:0045736; P:negative regulation of cyclin-dependent protein kinase activity
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter
GO:0018105; P:peptidyl-serine phosphorylation
GO:0040038; P:polar body extrusion after meiotic divisions
GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation
GO:0031648; P:protein destabilization
GO:0071168; P:protein localization to chromatin
GO:0016567; P:protein ubiquitination
GO:0090007; P:regulation of mitotic anaphase
GO:0043393; P:regulation of protein binding
GO:0046677; P:response to antibiotic
KEGG
hsa:5347;
InterPros
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.
Pfam
PF00069; Pkinase; 1.
PF00659; POLO_box; 2.
SMARTs
SM00220; S_TKc; 1.
Prosites
PS50078; POLO_BOX; 2.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Prints
Created Date20-Feb-2013