EKS-HOS-00269
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00269
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
Other/PLK416.71.8E-12462314253
StatusReviewed
Ensembl ProteinENSP00000361275
UniProt AccessionQ9H4B4; Q15767; Q5JR99; Q96CV1;
Protein NameSerine/threonine-protein kinase PLK3
Protein Synonyms/Alias Cytokine-inducible serine/threonine-protein kinase; FGF-inducible kinase; Polo-like kinase 3; PLK-3; Proliferation-related kinase;
Gene NamePLK3
Gene Synonyms/Alias PLK3; CNK, FNK, PRK;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000173846ENSP00000361275ENST00000372201
OrganismHomo sapiens
Functional DescriptionSerine/threonine-protein kinase involved in cell cycleregulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1.
Protein Length646
Protein Sequence
(FASTA)
MEPAAGFLSP RPFQRAAAAP APPAGPGPPP SALRGPELEM LAGLPTSDPG RLITDPRSGR 60
TYLKGRLLGK GGFARCYEAT DTETGSAYAV KVIPQSRVAK PHQREKILNE IELHRDLQHR 120
HIVRFSHHFE DADNIYIFLE LCSRKSLAHI WKARHTLLEP EVRYYLRQIL SGLKYLHQRG 180
ILHRDLKLGN FFITENMELK VGDFGLAARL EPPEQRKKTI CGTPNYVAPE VLLRQGHGPE 240
ADVWSLGCVM YTLLCGSPPF ETADLKETYR CIKQVHYTLP ASLSLPARQL LAAILRASPR 300
DRPSIDQILR HDFFTKGYTP DRLPISSCVT VPDLTPPNPA RSLFAKVTKS LFGRKKKSKN 360
HAQERDEVSG LVSGLMRTSV GHQDARPEAP AASGPAPVSL VETAPEDSSP RGTLASSGDG 420
FEEGLTVATV VESALCALRN CIAFMPPAEQ NPAPLAQPEP LVWVSKWVDY SNKFGFGYQL 480
SSRRVAVLFN DGTHMALSAN RKTVHYNPTS TKHFSFSVGA VPRALQPQLG ILRYFASYME 540
QHLMKGGDLP SVEEVEVPAP PLLLQWVKTD QALLMLFSDG TVQVNFYGDH TKLILSGWEP 600
LLVTFVARNR SACTYLASHL RQLGCSPDLR QRLRYALRLL RDRSPA 646
Nucleotide Sequence
(FASTA)
ATGGAGCCTG CCGCCGGTTT CCTGTCTCCG CGCCCCTTCC AGCGTGCGGC CGCCGCGCCC 60
GCTCCCCCGG CCGGGCCCGG GCCGCCTCCG AGTGCCTTGC GCGGACCTGA GCTGGAGATG 120
CTGGCCGGGC TACCGACGTC AGACCCCGGG CGCCTCATCA CGGACCCGCG CAGCGGCCGC 180
ACCTACCTCA AAGGCCGCTT GTTGGGCAAG GGGGGCTTCG CCCGCTGCTA CGAGGCCACT 240
GACACAGAGA CTGGCAGCGC CTACGCTGTC AAAGTCATCC CGCAGAGCCG CGTCGCCAAG 300
CCGCATCAGC GCGAGAAGAT CCTAAATGAG ATTGAGCTGC ACCGAGACCT GCAGCACCGC 360
CACATCGTGC GTTTTTCGCA CCACTTTGAG GACGCTGACA ACATCTACAT TTTCTTGGAG 420
CTCTGCAGCC GAAAGTCCCT GGCCCACATC TGGAAGGCCC GGCACACCCT GTTGGAGCCA 480
GAAGTGCGCT ACTACCTGCG GCAGATCCTT TCTGGCCTCA AGTACTTGCA CCAGCGCGGC 540
ATCTTGCACC GGGACCTCAA GTTGGGAAAT TTTTTCATCA CTGAGAACAT GGAACTGAAG 600
GTGGGGGATT TTGGGCTGGC AGCCCGGTTG GAGCCTCCGG AGCAGAGGAA GAAGACCATC 660
TGTGGCACCC CCAACTATGT GGCTCCAGAA GTGCTGCTGA GACAGGGCCA CGGCCCTGAG 720
GCGGATGTAT GGTCACTGGG CTGTGTCATG TACACGCTGC TCTGCGGGAG CCCTCCCTTT 780
GAGACGGCTG ACCTGAAGGA GACGTACCGC TGCATCAAGC AGGTTCACTA CACGCTGCCT 840
GCCAGCCTCT CACTGCCTGC CCGGCAGCTC CTGGCCGCCA TCCTTCGGGC CTCACCCCGA 900
GACCGCCCCT CTATTGACCA GATCCTGCGC CATGACTTCT TTACCAAGGG CTACACCCCC 960
GATCGACTCC CTATCAGCAG CTGCGTGACA GTCCCAGACC TGACACCCCC CAACCCAGCT 1020
AGGAGTCTGT TTGCCAAAGT TACCAAGAGC CTCTTTGGCA GAAAGAAGAA GAGTAAGAAT 1080
CATGCCCAGG AGAGGGATGA GGTCTCCGGT TTGGTGAGCG GCCTCATGCG CACATCCGTT 1140
GGCCATCAGG ATGCCAGGCC AGAGGCTCCA GCAGCTTCTG GCCCAGCCCC TGTCAGCCTG 1200
GTAGAGACAG CACCTGAAGA CAGCTCACCC CGTGGGACAC TGGCAAGCAG TGGAGATGGA 1260
TTTGAAGAAG GTCTGACTGT GGCCACAGTA GTGGAGTCAG CCCTTTGTGC TCTGAGAAAT 1320
TGTATAGCCT TCATGCCCCC AGCGGAACAG AACCCGGCCC CCCTGGCCCA GCCAGAGCCT 1380
CTGGTGTGGG TCAGCAAGTG GGTTGACTAC TCCAATAAGT TCGGCTTTGG GTATCAACTG 1440
TCCAGCCGCC GTGTGGCTGT GCTCTTCAAC GATGGCACAC ATATGGCCCT GTCGGCCAAC 1500
AGAAAGACTG TGCACTACAA TCCCACCAGC ACAAAGCACT TCTCCTTCTC CGTGGGTGCT 1560
GTGCCCCGGG CCCTGCAGCC TCAGCTGGGT ATCCTGCGGT ACTTCGCCTC CTACATGGAG 1620
CAGCACCTCA TGAAGGGTGG AGATCTGCCC AGTGTGGAAG AGGTAGAGGT ACCTGCTCCG 1680
CCCTTGCTGC TGCAGTGGGT CAAGACGGAT CAGGCTCTCC TCATGCTGTT TAGTGATGGC 1740
ACTGTCCAGG TGAACTTCTA CGGGGACCAC ACCAAGCTGA TTCTCAGTGG CTGGGAGCCC 1800
CTCCTTGTGA CTTTTGTGGC CCGAAATCGT AGTGCTTGTA CTTACCTCGC TTCCCACCTT 1860
CGGCAGCTGG GCTGCTCTCC AGACCTGCGG CAGCGACTCC GCTATGCTCT GCGCCTGCTC 1920
CGGGACCGCA GCCCAGCCTA G 1941
Domain Profile
S: 1     yergkllGkGgfakcyelkdletkevfavkvvpksllakekqrekvekeieihrslkhkn  60
         y +g+llGkGgfa+cye++d+et++++avkv+p+s++ak++qrek+ +eie+hr+l+h++
Q: 62    YLKGRLLGKGGFARCYEATDTETGSAYAVKVIPQSRVAKPHQREKILNEIELHRDLQHRH  121
         889*********************************************************
S: 61    ivklyeffedkenvylvlelcsrrslaellkrrkaltepevryylrqivsglkylhekri  120
         iv+++++fed++n+y++lelcsr+sla+++k+r++l epevryylrqi+sglkylh++ i
Q: 122   IVRFSHHFEDADNIYIFLELCSRKSLAHIWKARHTLLEPEVRYYLRQILSGLKYLHQRGI  181
         ************************************************************
S: 121   lhrdlklgnlflneelevkigdfGlatrlekeeerkktlcGtPnyiaPevlskkghslev  180
         lhrdlklgn+f++e++e+k+gdfGla+rle++e+rkkt+cGtPny+aPevl ++gh+ e+
Q: 182   LHRDLKLGNFFITENMELKVGDFGLAARLEPPEQRKKTICGTPNYVAPEVLLRQGHGPEA  241
         ************************************************************
S: 181   diWslGcilytllvGkPPfetkelketyekikkaeyslPsslskeaksliakllkkePee  240
         d+WslGc++ytll+G+PPfet++lkety++ik+ +y+lP+sls +a++l+a++l+++P++
Q: 242   DVWSLGCVMYTLLCGSPPFETADLKETYRCIKQVHYTLPASLSLPARQLLAAILRASPRD  301
         ************************************************************
S: 241   rpsleevlkdefl  253
         rps++++l+++f+
Q: 302   RPSIDQILRHDFF  314
         ************8
Domain Sequence
(FASTA)
YLKGRLLGKG GFARCYEATD TETGSAYAVK VIPQSRVAKP HQREKILNEI ELHRDLQHRH 60
IVRFSHHFED ADNIYIFLEL CSRKSLAHIW KARHTLLEPE VRYYLRQILS GLKYLHQRGI 120
LHRDLKLGNF FITENMELKV GDFGLAARLE PPEQRKKTIC GTPNYVAPEV LLRQGHGPEA 180
DVWSLGCVMY TLLCGSPPFE TADLKETYRC IKQVHYTLPA SLSLPARQLL AAILRASPRD 240
RPSIDQILRH DFF 253
KeywordApoptosis; ATP-binding; Cell cycle; Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; Golgi apparatus; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Ciona intestinalis"; ?>Danio rerio"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Macropus eugenii"; ?>Meleagris gallopavo"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Oreochromis niloticus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pteropus vampyrus"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00245
EKS-ANC-00251
EKS-BOT-00262
EKS-CAJ-00268
EKS-CAF-00269
EKS-CAP-00297
EKS-CII-00157
EKS-DAR-00597
EKS-EQC-00253
EKS-FEC-00248
EKS-GAM-00162
EKS-GAG-00219
EKS-GAA-00323
EKS-GOG-00260
EKS-ICT-00247
EKS-LAC-00274
EKS-LOA-00272
EKS-MAM-00264
EKS-MAE-00013
EKS-MEG-00206
EKS-MOD-00261
EKS-MUM-00293
EKS-MUP-00259
EKS-ORN-00339
EKS-ORC-00248
EKS-ORL-00316
EKS-OTG-00268
EKS-PAT-00249
EKS-PTV-00033
EKS-RAN-00277
EKS-SAH-00246
EKS-SUS-00227
EKS-TAG-00277
EKS-TAR-00336
EKS-TEN-00330
EKS-XET-00337
EKS-XIM-00331
Gene Ontology
GO:0005813; C:centrosome
GO:0030425; C:dendrite
GO:0005795; C:Golgi stack
GO:0043025; C:neuronal cell body
GO:0005730; C:nucleolus
GO:0005524; F:ATP binding
GO:0002039; F:p53 binding
GO:0004674; F:protein serine/threonine kinase activity
GO:0006915; P:apoptotic process
GO:0000910; P:cytokinesis
GO:0007113; P:endomitotic cell cycle
GO:0071779; P:G1/S transition checkpoint
GO:0000082; P:G1/S transition of mitotic cell cycle
GO:0090166; P:Golgi disassembly
GO:0071780; P:mitotic cell cycle G2/M transition checkpoint
GO:0043066; P:negative regulation of apoptotic process
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter
GO:2000777; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia
GO:0043491; P:protein kinase B signaling cascade
GO:0006974; P:response to DNA damage stimulus
GO:0006970; P:response to osmotic stress
GO:0009314; P:response to radiation
GO:0000302; P:response to reactive oxygen species
GO:0000084; P:S phase of mitotic cell cycle
KEGG
hsa:1263;
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.
IPR020658; Ser/Thr_kinase_Plk3.
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