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Serine/threonine-protein kinase plk-1 (EC 2.7.11.21) (Polo-like kinase 1)

 PLK1_CAEEL              Reviewed;         649 AA.
P34331; O61662; O76763;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
25-NOV-2002, sequence version 3.
12-SEP-2018, entry version 166.
RecName: Full=Serine/threonine-protein kinase plk-1;
EC=2.7.11.21;
AltName: Full=Polo-like kinase 1;
Name=plk-1; Synonyms=plc1; ORFNames=C14B9.4;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
PubMed=10376213; DOI=10.3109/10425179909008427;
Ouyang B., Wang Y., Dai W.;
"Caenorhabditis elegans contains structural homologs of human prk and
plk.";
DNA Seq. 10:109-113(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND SUBCELLULAR
LOCATION.
STRAIN=Bristol N2;
PubMed=10660671;
DOI=10.1002/(SICI)1526-968X(200001)26:1<26::AID-GENE6>3.0.CO;2-O;
Chase D., Serafinas C., Ashcroft N., Kosinski M., Longo D.,
Ferris D.K., Golden A.;
"The polo-like kinase PLK-1 is required for nuclear envelope breakdown
and the completion of meiosis in Caenorhabditis elegans.";
Genesis 26:26-41(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=7906398; DOI=10.1038/368032a0;
Wilson R., Ainscough R., Anderson K., Baynes C., Berks M.,
Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A.,
Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A.,
Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M.,
Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N.,
Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M.,
Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R.,
Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R.,
Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K.,
Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J.,
Wohldman P.;
"2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
elegans.";
Nature 368:32-38(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[5]
FUNCTION, INTERACTION WITH MEX-5 AND MEX-6, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, AND DOMAIN.
PubMed=18199581; DOI=10.1242/dev.013425;
Nishi Y., Rogers E., Robertson S.M., Lin R.;
"Polo kinases regulate C. elegans embryonic polarity via binding to
DYRK2-primed MEX-5 and MEX-6.";
Development 135:687-697(2008).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18305005; DOI=10.1242/dev.019075;
Budirahardja Y., Gonczy P.;
"PLK-1 asymmetry contributes to asynchronous cell division of C.
elegans embryos.";
Development 135:1303-1313(2008).
[7]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
PubMed=18316412; DOI=10.1083/jcb.200710018;
Rivers D.M., Moreno S., Abraham M., Ahringer J.;
"PAR proteins direct asymmetry of the cell cycle regulators Polo-like
kinase and Cdc25.";
J. Cell Biol. 180:877-885(2008).
[8]
FUNCTION, INTERACTION WITH SPAT-1, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=20823068; DOI=10.1242/dev.055293;
Noatynska A., Panbianco C., Gotta M.;
"SPAT-1/Bora acts with Polo-like kinase 1 to regulate PAR polarity and
cell cycle progression.";
Development 137:3315-3325(2010).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=22018922; DOI=10.1016/j.devcel.2011.09.001;
Harper N.C., Rillo R., Jover-Gil S., Assaf Z.J., Bhalla N.,
Dernburg A.F.;
"Pairing centers recruit a Polo-like kinase to orchestrate meiotic
chromosome dynamics in C. elegans.";
Dev. Cell 21:934-947(2011).
-!- FUNCTION: Required for oocyte nuclear envelope breakdown before
entry of oocyte into spermatheca (PubMed:10660671). In meiotic
cells, required for spindle dynamics and probably for spindle
attachment to the chromosomes (PubMed:10660671). Zygotic role in
the development of the germline and nerve cord (PubMed:10660671).
In mitotic cells, plays a role in spindle organization and
centrosome maturation (PubMed:20823068). Involved in asymmetric
nuclear localization of cdc-25.1 during embryogenesis which
affects cell division timing (PubMed:18305005, PubMed:18316412,
PubMed:20823068). Together with plk-2, regulates cytoplasm
polarity in early embryos (PubMed:18199581, PubMed:18316412,
PubMed:18305005). May play a minor role in chromosome pairing and
synapsis during oocyte meiosis I (PubMed:22018922).
{ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:18199581,
ECO:0000269|PubMed:18305005, ECO:0000269|PubMed:18316412,
ECO:0000269|PubMed:20823068, ECO:0000269|PubMed:22018922}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with mex-5, mex-6 and spat-1.
{ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:20823068}.
-!- INTERACTION:
P91349:spd-5; NbExp=3; IntAct=EBI-315211, EBI-322479;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:10660671,
ECO:0000269|PubMed:18305005, ECO:0000269|PubMed:22018922}. Midbody
{ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:18305005}.
Cytoplasm {ECO:0000269|PubMed:18199581,
ECO:0000269|PubMed:18305005, ECO:0000269|PubMed:18316412,
ECO:0000269|PubMed:20823068, ECO:0000269|PubMed:22018922}. Nucleus
{ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:22018922}.
Chromosome {ECO:0000269|PubMed:10660671,
ECO:0000269|PubMed:22018922}. Chromosome, centromere, kinetochore
{ECO:0000269|PubMed:22018922}. Note=In mitosis, remains associated
with centrosomes entering prophase through to anaphase. During
metaphase, embryos show anterior enrichment and located to the
chromosomes of the metaphase plate. In meiosis, detected at
centrosomes after pronuclear meeting in post-meiotic 1-cell
embryos. Associated with chromatin during chromosome segregation
of anaphase and in the region between the dividing chromosomes.
Cytoplasmic in mature, unfertilized oocytes (PubMed:10660671).
Asymmetric cytoplasmic localization is regulated by mex-5 and mex-
6 (PubMed:18199581, PubMed:18316412).
{ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:18199581,
ECO:0000269|PubMed:18316412}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=b;
IsoId=P34331-1; Sequence=Displayed;
Name=a;
IsoId=P34331-2; Sequence=VSP_004928;
-!- TISSUE SPECIFICITY: Embryos. {ECO:0000269|PubMed:18199581,
ECO:0000269|PubMed:20823068}.
-!- DOMAIN: The POLO box domains are involved in the asymmetric
cytoplasmic localization. {ECO:0000269|PubMed:18199581,
ECO:0000269|PubMed:18316412}.
-!- DISRUPTION PHENOTYPE: Impaired protein polarity (PubMed:18316412,
PubMed:20823068). Lengthened AB and P1 cell cycle times
(PubMed:18316412, PubMed:20823068). RNAi-mediated knockdown causes
defects in germline mitosis including cell-cylce arrest and
formation of polyploid nuclei (PubMed:22018922). RNAi-mediated
knockdown in plk-2 mutant background causes a loss in sun-1
phosphorylation at 'Ser-8' but not at 'Ser-12' (PubMed:22018922).
{ECO:0000269|PubMed:18316412, ECO:0000269|PubMed:20823068,
ECO:0000269|PubMed:22018922}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; AF057165; AAC14129.1; -; mRNA.
EMBL; AF080581; AAC34661.1; -; mRNA.
EMBL; FO080531; CCD64438.1; -; Genomic_DNA.
EMBL; FO080531; CCD64439.1; -; Genomic_DNA.
PIR; A88520; A88520.
PIR; T43337; T43337.
RefSeq; NP_001021173.1; NM_001026002.2. [P34331-2]
RefSeq; NP_001021174.1; NM_001026003.2. [P34331-1]
UniGene; Cel.18095; -.
ProteinModelPortal; P34331; -.
SMR; P34331; -.
BioGrid; 41349; 16.
DIP; DIP-25456N; -.
IntAct; P34331; 14.
STRING; 6239.C14B9.4b; -.
iPTMnet; P34331; -.
EPD; P34331; -.
PaxDb; P34331; -.
PeptideAtlas; P34331; -.
PRIDE; P34331; -.
EnsemblMetazoa; C14B9.4b; C14B9.4b; WBGene00004042. [P34331-1]
GeneID; 176143; -.
KEGG; cel:CELE_C14B9.4; -.
UCSC; C14B9.4a.1; c. elegans. [P34331-1]
CTD; 176143; -.
WormBase; C14B9.4a; CE26649; WBGene00004042; plk-1. [P34331-2]
WormBase; C14B9.4b; CE30602; WBGene00004042; plk-1. [P34331-1]
eggNOG; KOG0575; Eukaryota.
eggNOG; ENOG410XQBP; LUCA.
GeneTree; ENSGT00530000062954; -.
HOGENOM; HOG000248546; -.
InParanoid; P34331; -.
KO; K06631; -.
OMA; FEVDTWS; -.
OrthoDB; EOG091G0D89; -.
PhylomeDB; P34331; -.
BRENDA; 2.7.11.21; 1045.
Reactome; R-CEL-156711; Polo-like kinase mediated events.
Reactome; R-CEL-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
Reactome; R-CEL-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-CEL-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-CEL-68884; Mitotic Telophase/Cytokinesis.
SignaLink; P34331; -.
PRO; PR:P34331; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00004042; Expressed in 5 organ(s), highest expression level in germ line (C elegans).
GO; GO:0005813; C:centrosome; IDA:WormBase.
GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0051233; C:spindle midzone; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:WormBase.
GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
GO; GO:0007147; P:female meiosis II; IMP:UniProtKB.
GO; GO:0045132; P:meiotic chromosome segregation; IMP:WormBase.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; IMP:UniProtKB.
GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:WormBase.
GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
GO; GO:0051726; P:regulation of cell cycle; IMP:WormBase.
CDD; cd13118; POLO_box_1; 1.
CDD; cd13117; POLO_box_2; 1.
Gene3D; 3.30.1120.30; -; 3.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR033701; POLO_box_1.
InterPro; IPR033695; POLO_box_2.
InterPro; IPR000959; POLO_box_dom.
InterPro; IPR036947; POLO_box_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00659; POLO_box; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50078; POLO_BOX; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell cycle; Cell division;
Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton;
Kinase; Kinetochore; Meiosis; Mitosis; Nucleotide-binding; Nucleus;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 649 Serine/threonine-protein kinase plk-1.
/FTId=PRO_0000086569.
DOMAIN 38 290 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 420 485 POLO box 1. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
DOMAIN 520 589 POLO box 2. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
NP_BIND 44 52 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 162 162 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 67 67 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
VAR_SEQ 83 89 VDNERIL -> MTQEVQ (in isoform a).
{ECO:0000303|PubMed:10660671}.
/FTId=VSP_004928.
SEQUENCE 649 AA; 73633 MW; 54D969F140D7A43B CRC64;
MNRLPNIAKP PQKSNQRKEK APPEVPALIA DKDRGTYYEK GRFLGKGGFA HCYELTNRAT
REVVAGKVVP KSMLVKQYQR DKVDNERILI HRELGHINIV KLFNFFEDNL NVYITLELCA
RRSLMELHKR RKAVTEPEAR YFTHQIVDGV LYLHDLNIIH RDMKLGNLFL NDDLVVKIGD
FGLATTVNGD ERKKTLCGTP NYIAPEVLNK AGHSFEVDIW AVGCILYILL FGQPPFESKS
LEETYSRIRH NNYTIPSIAT QPAASLIRKM LDPEPTRRPT AKQVQRDGFF KSGFMPTRLP
VSCLTMVPKF GGHETSMMEE NVAPRGVDAR SQRPLNGRAG LSALPQHIVS NNADRERAQQ
QAAEATFREP EDAYLSQLFH QVAVLLEQRI PGLEEEEAAL DGYQSPECLP VFWISKWVDY
SDKYGIGYQL CDNSVGVLFN DNSRIMLDQA GNELTYIEKS NKEHYFSMHS GEMPGLLNKK
VTLLKYFRSY MNDHLVKAGE GSEQRAGDDL ARLPTLRVWF RTKSAIVLHL SNGTVQINFF
NDHVKMMMCP LMQAVTFIDQ NKRMLTYKLN NLQRNGCPEK FLHRLKYAKT MIERLMSDAN
VVSQNPARQP DMPRSMAAAR SASAGSRGPN QAASHLPQSA SGSNIHPRR


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