EKS-MUM-00291
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-MUM-00291
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
Other/PLK428.12.8E-12853305253
StatusReviewed
Ensembl ProteinENSMUSP00000033154
UniProt AccessionQ07832;
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
ENSMUSG00000030867ENSMUSP00000033154ENSMUST00000033154
OrganismMus musculus
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 (By similarity).
Protein Length603
Protein Sequence
(FASTA)
MNAAAKAGKL ARAPADLGKG GVPGDAVPGA PVAAPLAKEI PEVLVDPRSR RQYVRGRFLG 60
KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQKEKMSM EISIHRSLAH QHVVGFHDFF 120
EDSDFVFVVL ELCRRRSLLE LHKRRKALTE PEARYYLRQI VLGCQYLHRN QVIHRDLKLG 180
NLFLNEDLEV KIGDFGLATK VEYEGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI 240
MYTLLVGKPP FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTIHELL 300
NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSSRKPL KVLNKGVENP LPDRPREKEE 360
PVVRETNEAI ECHLSDLLQQ LTSVNASKPS ERGLVRQEEA EDPACIPIFW VSKWVDYSDK 420
YGLGYQLCDN SVGVLFNDST RLILYNDGDS LQYIERDGTE SYLTVSSHPN SLMKKITLLN 480
YFRNYMSEHL LKAGANITPR EGDELARLPY LRTWFRTRSA IILHLSNGTV QINFFQDHTK 540
LILCPLMAAV TYINEKRDFQ TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL 600
KAS 603
Nucleotide Sequence
(FASTA)
ATGAATGCAG CGGCCAAAGC TGGAAAGCTG GCTCGAGCAC CAGCCGACCT CGGGAAAGGT 60
GGGGTTCCGG GAGATGCAGT TCCCGGTGCC CCAGTGGCCG CCCCGCTGGC GAAAGAAATT 120
CCGGAGGTCC TAGTGGACCC ACGCAGCCGG CGGCAGTATG TACGGGGGCG CTTTCTGGGT 180
AAAGGAGGCT TCGCCAAATG CTTCGAGATC TCAGACGCAG ACACAAAAGA GGTGTTCGCA 240
GGCAAGATCG TGCCTAAGTC TTTGCTGCTC AAGCCCCACC AGAAGGAGAA GATGTCTATG 300
GAGATCTCAA TTCACCGCAG CCTAGCACAC CAACACGTCG TAGGCTTCCA TGACTTTTTT 360
GAGGACAGCG ACTTTGTATT TGTAGTTTTG GAGCTCTGTC GCAGGAGGTC CCTCCTGGAG 420
CTGCACAAGA GGAGGAAGGC ACTGACCGAG CCTGAGGCCC GCTACTACCT GCGACAGATA 480
GTCCTGGGCT GCCAGTACCT GCACCGCAAT CAGGTCATTC ACAGGGACCT CAAGCTGGGC 540
AACCTCTTCC TGAACGAGGA TCTGGAGGTG AAAATAGGGG ATTTTGGCTT GGCAACCAAA 600
GTGGAATATG AAGGGGAACG AAAGAAGACC TTGTGTGGCA CTCCTAACTA CATAGCTCCT 660
GAGGTGCTGA GCAAGAAGGG ACACAGTTTT GAGGTGGATG TGTGGTCCAT TGGGTGCATC 720
ATGTATACCT TGCTAGTGGG CAAGCCTCCC TTTGAGACCT CGTGCCTAAA AGAGACCTAC 780
CTCCGGATCA AGAAAAATGA ATACAGTATT CCCAAGCACA TCAACCCAGT GGCCGCCTCC 840
CTCATCCAGA AGATGCTTCA GACAGACCCC ACTGCCCGCC CCACCATTCA CGAGTTGCTC 900
AATGACGAGT TCTTCACTTC TGGCTACATC CCCGCCCGTC TCCCTATTAC CTGCCTCACC 960
ATCCCACCAA GGTTTTCAAT CGCTCCCAGC AGCCTGGACC CCAGCAGCAG GAAACCTCTC 1020
AAAGTCCTCA ATAAAGGTGT GGAGAACCCC CTGCCTGACC GTCCCCGGGA GAAAGAGGAA 1080
CCGGTGGTCC GGGAGACAAA TGAGGCCATT GAGTGCCACC TTAGTGACTT GCTACAGCAG 1140
CTGACCAGTG TCAACGCCTC CAAGCCCTCG GAGCGCGGGC TGGTGCGGCA AGAGGAGGCT 1200
GAGGATCCTG CCTGCATCCC CATCTTCTGG GTCAGCAAGT GGGTGGACTA TTCGGACAAG 1260
TATGGCCTTG GGTATCAGCT GTGTGACAAC AGTGTGGGGG TGCTTTTTAA TGACTCAACA 1320
CGCCTGATTC TCTACAATGA CGGGGACAGC CTGCAGTACA TAGAGCGTGA TGGCACGGAG 1380
TCCTATCTCA CTGTGAGCTC CCATCCCAAT TCCTTGATGA AGAAGATCAC TCTCCTCAAC 1440
TATTTCCGCA ATTACATGAG TGAGCACCTG CTGAAGGCAG GGGCCAACAT CACACCCCGG 1500
GAAGGCGACG AGCTGGCCCG GCTGCCCTAC CTACGAACGT GGTTCCGCAC ACGCAGCGCC 1560
ATCATCCTGC ACCTCAGCAA CGGCACCGTG CAGATTAACT TCTTCCAGGA CCACACCAAA 1620
CTTATCCTGT GCCCCCTGAT GGCAGCGGTG ACCTACATCA ACGAGAAGAG GGACTTCCAA 1680
ACGTACCGCC TGAGCCTCCT GGAGGAGTAT GGCTGCTGCA AGGAGCTGGC CAGCCGCCTC 1740
CGCTACGCCC GCACCATGGT AGACAAGCTG CTGAGCTCGC GCTCCGCCAG CAACCGCCTC 1800
AAGGCCTCCT AG 1812
Domain Profile
S: 1     yergkllGkGgfakcyelkdletkevfavkvvpksllakekqrekvekeieihrslkhkn  60
         y rg++lGkGgfakc+e++d++tkevfa k+vpksll k++q+ek+++ei+ihrsl+h++
Q: 53    YVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQKEKMSMEISIHRSLAHQH  112
         89**********************************************************
S: 61    ivklyeffedkenvylvlelcsrrslaellkrrkaltepevryylrqivsglkylhekri  120
         +v +++ffed+++v++vlelc+rrsl el+krrkaltepe+ryylrqiv g++ylh++++
Q: 113   VVGFHDFFEDSDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNQV  172
         ************************************************************
S: 121   lhrdlklgnlflneelevkigdfGlatrlekeeerkktlcGtPnyiaPevlskkghslev  180
         +hrdlklgnlflne+levkigdfGlat++e+e+erkktlcGtPnyiaPevlskkghs+ev
Q: 173   IHRDLKLGNLFLNEDLEVKIGDFGLATKVEYEGERKKTLCGTPNYIAPEVLSKKGHSFEV  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   RPTIHELLNDEFF  305
         ************8
Domain Sequence
(FASTA)
YVRGRFLGKG GFAKCFEISD ADTKEVFAGK IVPKSLLLKP HQKEKMSMEI SIHRSLAHQH 60
VVGFHDFFED SDFVFVVLEL CRRRSLLELH KRRKALTEPE ARYYLRQIVL GCQYLHRNQV 120
IHRDLKLGNL FLNEDLEVKI GDFGLATKVE YEGERKKTLC GTPNYIAPEV LSKKGHSFEV 180
DVWSIGCIMY TLLVGKPPFE TSCLKETYLR IKKNEYSIPK HINPVAASLI QKMLQTDPTA 240
RPTIHELLND EFF 253
KeywordATP-binding; Cell cycle; Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Kinetochore; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; 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"; ?>Homo sapiens"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Macropus eugenii"; ?>Meleagris gallopavo"; ?>Microcebus murinus"; ?>Monodelphis domestica"; ?>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"; ?>Saccharomyces cerevisiae"; ?>
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-HOS-00268
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-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
EKS-SAC-00030
Gene Ontology
GO:0005813; C:centrosome
GO:0000942; C:condensed nuclear chromosome outer kinetochore
GO:0000776; C:kinetochore
GO:0030496; C:midbody
GO:0005634; C:nucleus
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: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:0000236; P:mitotic prometaphase
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
mmu:18817;
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