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PLK1_CAEEL
ID   PLK1_CAEEL              Reviewed;         649 AA.
AC   P34331; O61662; O76763;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2002, sequence version 3.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Serine/threonine-protein kinase plk-1;
DE            EC=2.7.11.21;
DE   AltName: Full=Polo-like kinase 1;
GN   Name=plk-1; Synonyms=plc1; ORFNames=C14B9.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RX   PubMed=10376213; DOI=10.3109/10425179909008427;
RA   Ouyang B., Wang Y., Dai W.;
RT   "Caenorhabditis elegans contains structural homologs of human prk and
RT   plk.";
RL   DNA Seq. 10:109-113(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=Bristol N2;
RX   PubMed=10660671;
RX   DOI=10.1002/(sici)1526-968x(200001)26:1<26::aid-gene6>3.0.co;2-o;
RA   Chase D., Serafinas C., Ashcroft N., Kosinski M., Longo D., Ferris D.K.,
RA   Golden A.;
RT   "The polo-like kinase PLK-1 is required for nuclear envelope breakdown and
RT   the completion of meiosis in Caenorhabditis elegans.";
RL   Genesis 26:26-41(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [5]
RP   FUNCTION, INTERACTION WITH MEX-5 AND MEX-6, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DOMAIN.
RX   PubMed=18199581; DOI=10.1242/dev.013425;
RA   Nishi Y., Rogers E., Robertson S.M., Lin R.;
RT   "Polo kinases regulate C. elegans embryonic polarity via binding to DYRK2-
RT   primed MEX-5 and MEX-6.";
RL   Development 135:687-697(2008).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18305005; DOI=10.1242/dev.019075;
RA   Budirahardja Y., Gonczy P.;
RT   "PLK-1 asymmetry contributes to asynchronous cell division of C. elegans
RT   embryos.";
RL   Development 135:1303-1313(2008).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX   PubMed=18316412; DOI=10.1083/jcb.200710018;
RA   Rivers D.M., Moreno S., Abraham M., Ahringer J.;
RT   "PAR proteins direct asymmetry of the cell cycle regulators Polo-like
RT   kinase and Cdc25.";
RL   J. Cell Biol. 180:877-885(2008).
RN   [8]
RP   FUNCTION, INTERACTION WITH SPAT-1, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=20823068; DOI=10.1242/dev.055293;
RA   Noatynska A., Panbianco C., Gotta M.;
RT   "SPAT-1/Bora acts with Polo-like kinase 1 to regulate PAR polarity and cell
RT   cycle progression.";
RL   Development 137:3315-3325(2010).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22018922; DOI=10.1016/j.devcel.2011.09.001;
RA   Harper N.C., Rillo R., Jover-Gil S., Assaf Z.J., Bhalla N., Dernburg A.F.;
RT   "Pairing centers recruit a Polo-like kinase to orchestrate meiotic
RT   chromosome dynamics in C. elegans.";
RL   Dev. Cell 21:934-947(2011).
CC   -!- FUNCTION: Required for oocyte nuclear envelope breakdown before entry
CC       of oocyte into spermatheca (PubMed:10660671). In meiotic cells,
CC       required for spindle dynamics and probably for spindle attachment to
CC       the chromosomes (PubMed:10660671). Zygotic role in the development of
CC       the germline and nerve cord (PubMed:10660671). In mitotic cells, plays
CC       a role in spindle organization and centrosome maturation
CC       (PubMed:20823068). Involved in asymmetric nuclear localization of cdc-
CC       25.1 during embryogenesis which affects cell division timing
CC       (PubMed:18305005, PubMed:18316412, PubMed:20823068). Together with plk-
CC       2, regulates cytoplasm polarity in early embryos (PubMed:18199581,
CC       PubMed:18316412, PubMed:18305005). May play a minor role in chromosome
CC       pairing and synapsis during oocyte meiosis I (PubMed:22018922).
CC       {ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:18199581,
CC       ECO:0000269|PubMed:18305005, ECO:0000269|PubMed:18316412,
CC       ECO:0000269|PubMed:20823068, ECO:0000269|PubMed:22018922}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.21;
CC   -!- SUBUNIT: Interacts with mex-5, mex-6 and spat-1.
CC       {ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:20823068}.
CC   -!- INTERACTION:
CC       P34331; P91349: spd-5; NbExp=3; IntAct=EBI-315211, EBI-322479;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000269|PubMed:10660671,
CC       ECO:0000269|PubMed:18305005, ECO:0000269|PubMed:22018922}. Midbody
CC       {ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:18305005}. Cytoplasm
CC       {ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:18305005,
CC       ECO:0000269|PubMed:18316412, ECO:0000269|PubMed:20823068,
CC       ECO:0000269|PubMed:22018922}. Nucleus {ECO:0000269|PubMed:10660671,
CC       ECO:0000269|PubMed:22018922}. Chromosome {ECO:0000269|PubMed:10660671,
CC       ECO:0000269|PubMed:22018922}. Chromosome, centromere, kinetochore
CC       {ECO:0000269|PubMed:22018922}. Note=In mitosis, remains associated with
CC       centrosomes entering prophase through to anaphase. During metaphase,
CC       embryos show anterior enrichment and located to the chromosomes of the
CC       metaphase plate. In meiosis, detected at centrosomes after pronuclear
CC       meeting in post-meiotic 1-cell embryos. Associated with chromatin
CC       during chromosome segregation of anaphase and in the region between the
CC       dividing chromosomes. Cytoplasmic in mature, unfertilized oocytes
CC       (PubMed:10660671). Asymmetric cytoplasmic localization is regulated by
CC       mex-5 and mex-6 (PubMed:18199581, PubMed:18316412).
CC       {ECO:0000269|PubMed:10660671, ECO:0000269|PubMed:18199581,
CC       ECO:0000269|PubMed:18316412}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=b;
CC         IsoId=P34331-1; Sequence=Displayed;
CC       Name=a;
CC         IsoId=P34331-2; Sequence=VSP_004928;
CC   -!- TISSUE SPECIFICITY: Embryos. {ECO:0000269|PubMed:18199581,
CC       ECO:0000269|PubMed:20823068}.
CC   -!- DOMAIN: The POLO box domains are involved in the asymmetric cytoplasmic
CC       localization. {ECO:0000269|PubMed:18199581,
CC       ECO:0000269|PubMed:18316412}.
CC   -!- DISRUPTION PHENOTYPE: Impaired protein polarity (PubMed:18316412,
CC       PubMed:20823068). Lengthened AB and P1 cell cycle times
CC       (PubMed:18316412, PubMed:20823068). RNAi-mediated knockdown causes
CC       defects in germline mitosis including cell-cylce arrest and formation
CC       of polyploid nuclei (PubMed:22018922). RNAi-mediated knockdown in plk-2
CC       mutant background causes a loss in sun-1 phosphorylation at 'Ser-8' but
CC       not at 'Ser-12' (PubMed:22018922). {ECO:0000269|PubMed:18316412,
CC       ECO:0000269|PubMed:20823068, ECO:0000269|PubMed:22018922}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; AF057165; AAC14129.1; -; mRNA.
DR   EMBL; AF080581; AAC34661.1; -; mRNA.
DR   EMBL; FO080531; CCD64438.1; -; Genomic_DNA.
DR   EMBL; FO080531; CCD64439.1; -; Genomic_DNA.
DR   PIR; A88520; A88520.
DR   PIR; T43337; T43337.
DR   RefSeq; NP_001021173.1; NM_001026002.2. [P34331-2]
DR   RefSeq; NP_001021174.1; NM_001026003.2.
DR   AlphaFoldDB; P34331; -.
DR   SMR; P34331; -.
DR   BioGRID; 41349; 44.
DR   DIP; DIP-25456N; -.
DR   IntAct; P34331; 14.
DR   STRING; 6239.C14B9.4b; -.
DR   iPTMnet; P34331; -.
DR   EPD; P34331; -.
DR   PaxDb; P34331; -.
DR   PeptideAtlas; P34331; -.
DR   EnsemblMetazoa; C14B9.4.1; C14B9.4.1; WBGene00004042. [P34331-2]
DR   GeneID; 176143; -.
DR   KEGG; cel:CELE_C14B9.4; -.
DR   UCSC; C14B9.4a.1; c. elegans. [P34331-1]
DR   CTD; 176143; -.
DR   WormBase; C14B9.4a; CE26649; WBGene00004042; plk-1. [P34331-2]
DR   WormBase; C14B9.4b; CE30602; WBGene00004042; plk-1. [P34331-1]
DR   eggNOG; KOG0575; Eukaryota.
DR   GeneTree; ENSGT00940000166918; -.
DR   HOGENOM; CLU_000288_46_1_1; -.
DR   InParanoid; P34331; -.
DR   OMA; LKHFERY; -.
DR   OrthoDB; 507604at2759; -.
DR   PhylomeDB; P34331; -.
DR   BRENDA; 2.7.11.21; 1045.
DR   PRO; PR:P34331; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00004042; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005813; C:centrosome; IDA:WormBase.
DR   GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0051233; C:spindle midzone; IDA:WormBase.
DR   GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR   GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR   GO; GO:0007147; P:female meiosis II; IMP:UniProtKB.
DR   GO; GO:0045132; P:meiotic chromosome segregation; IMP:WormBase.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0007077; P:mitotic nuclear membrane disassembly; IMP:UniProtKB.
DR   GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR   GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:WormBase.
DR   GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:WormBase.
DR   GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR   CDD; cd13118; POLO_box_1; 1.
DR   CDD; cd13117; POLO_box_2; 1.
DR   Gene3D; 3.30.1120.30; -; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033701; POLO_box_1.
DR   InterPro; IPR033695; POLO_box_2.
DR   InterPro; IPR000959; POLO_box_dom.
DR   InterPro; IPR036947; POLO_box_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00659; POLO_box; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50078; POLO_BOX; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell cycle; Cell division; Centromere;
KW   Chromosome; Cytoplasm; Cytoskeleton; Kinase; Kinetochore; Meiosis; Mitosis;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..649
FT                   /note="Serine/threonine-protein kinase plk-1"
FT                   /id="PRO_0000086569"
FT   DOMAIN          38..290
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          420..485
FT                   /note="POLO box 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT   DOMAIN          520..589
FT                   /note="POLO box 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         44..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   VAR_SEQ         83..89
FT                   /note="VDNERIL -> MTQEVQ (in isoform a)"
FT                   /evidence="ECO:0000303|PubMed:10660671"
FT                   /id="VSP_004928"
SQ   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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