PLK5_MOUSE
ID PLK5_MOUSE Reviewed; 595 AA.
AC Q4FZD7; Q0VGS4; Q8C096;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Inactive serine/threonine-protein kinase PLK5;
DE AltName: Full=Polo-like kinase 5;
DE Short=PLK-5;
GN Name=Plk5 {ECO:0000250|UniProtKB:Q64702};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC27628.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC27628.1};
RC TISSUE=Medulla oblongata {ECO:0000312|EMBL:BAC27628.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH99679.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH99679.1};
RC TISSUE=Eye {ECO:0000312|EMBL:AAH99679.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20100802; DOI=10.1093/nar/gkq011;
RA Andrysik Z., Bernstein W.Z., Deng L., Myer D.L., Li Y.Q., Tischfield J.A.,
RA Stambrook P.J., Bahassi el M.;
RT "The novel mouse Polo-like kinase 5 responds to DNA damage and localizes in
RT the nucleolus.";
RL Nucleic Acids Res. 38:2931-2943(2010).
RN [4]
RP FUNCTION, INDUCTION, AND MUTAGENESIS OF ASP-150 AND TRP-417.
RX PubMed=21245385; DOI=10.1128/mcb.00607-10;
RA de Carcer G., Escobar B., Higuero A.M., Garcia L., Anson A., Perez G.,
RA Mollejo M., Manning G., Melendez B., Abad-Rodriguez J., Malumbres M.;
RT "Plk5, a polo box domain-only protein with specific roles in neuron
RT differentiation and glioblastoma suppression.";
RL Mol. Cell. Biol. 31:1225-1239(2011).
CC -!- FUNCTION: Inactive serine/threonine-protein kinase that plays a role in
CC cell cycle progression and neuronal differentiation.
CC {ECO:0000269|PubMed:20100802, ECO:0000269|PubMed:21245385}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20100802}.
CC Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the cerebellum, eye and brain cortex
CC (at protein level). Expressed in highly differentiated tissues, such as
CC brain, eyes and ovary. Not detectable in proliferating tissues, such as
CC the colon, spleen and placenta.
CC -!- INDUCTION: Down-regulated in proliferating cells or in serum-stimulated
CC cells or growth factors. Up-regulated in asynchronous cells, or upon
CC serum deprivation or following stress inducible DNA damage treatment.
CC {ECO:0000269|PubMed:20100802, ECO:0000269|PubMed:21245385}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive; has lost the main activatory autophosphorylation site and the
CC conserved key residues involved in phospho-substrate. The C-terminal
CC region (containing the POLO box domain) is sufficient for inducing cell
CC cycle arrest (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH86684.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC27628.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK031968; BAC27628.1; ALT_FRAME; mRNA.
DR EMBL; BC086684; AAH86684.1; ALT_INIT; mRNA.
DR EMBL; BC099679; AAH99679.1; -; mRNA.
DR CCDS; CCDS83729.1; -.
DR RefSeq; NP_001334053.1; NM_001347124.1.
DR RefSeq; NP_898975.2; NM_183152.4.
DR AlphaFoldDB; Q4FZD7; -.
DR SMR; Q4FZD7; -.
DR STRING; 10090.ENSMUSP00000044400; -.
DR PhosphoSitePlus; Q4FZD7; -.
DR PaxDb; Q4FZD7; -.
DR PRIDE; Q4FZD7; -.
DR ProteomicsDB; 289687; -.
DR Antibodypedia; 64895; 182 antibodies from 29 providers.
DR DNASU; 216166; -.
DR Ensembl; ENSMUST00000105351; ENSMUSP00000100988; ENSMUSG00000035486.
DR GeneID; 216166; -.
DR KEGG; mmu:216166; -.
DR UCSC; uc007gcy.2; mouse.
DR CTD; 126520; -.
DR MGI; MGI:3026984; Plk5.
DR VEuPathDB; HostDB:ENSMUSG00000035486; -.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000162321; -.
DR InParanoid; Q4FZD7; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; Q4FZD7; -.
DR BRENDA; 2.7.11.21; 3474.
DR BioGRID-ORCS; 216166; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q4FZD7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q4FZD7; protein.
DR Bgee; ENSMUSG00000035486; Expressed in retinal neural layer and 57 other tissues.
DR ExpressionAtlas; Q4FZD7; baseline and differential.
DR Genevisible; Q4FZD7; MM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
DR GO; GO:0002357; P:defense response to tumor cell; IDA:UniProtKB.
DR GO; GO:0090166; P:Golgi disassembly; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0044819; P:mitotic G1/S transition checkpoint signaling; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR CDD; cd13118; POLO_box_1; 1.
DR Gene3D; 3.30.1120.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
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; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50078; POLO_BOX; 1.
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 ATP-binding; Cell cycle; Cell division; Cytoplasm; Differentiation;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..595
FT /note="Inactive serine/threonine-protein kinase PLK5"
FT /id="PRO_0000274545"
FT DOMAIN 27..279
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 420..483
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 326..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q13131,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 33..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13131,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13131,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 150
FT /note="D->A: Induces cell cycle arrest and neurite
FT differentiation."
FT /evidence="ECO:0000269|PubMed:21245385"
FT MUTAGEN 417
FT /note="W->A: Induces cell cycle arrest."
FT /evidence="ECO:0000269|PubMed:21245385"
FT CONFLICT 523
FT /note="V -> D (in Ref. 1; BAC27628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 66055 MW; 1BB8E6CBDF22B7CF CRC64;
MEPRSRRRRS RQLVATFLRD PGSGRVYRRG KLIGKGAFSR CYKLTDMSTS AVFALKVVPR
GGAGRLRLRG KVEREIALHS RLRHRNIVAF HAHFADRDHV YMVLEYCSRQ SLAHVLKVRR
TLTEPEVRYY LRGLVSGLRY LHQQRIVHRD LKPSNFFLNK NMEVKIGDLG LAARVGPAGR
CHRVLCGTPN FQAPEVVSRN GHSCKSDIWA LGCIMYTVLT GTPPFAAAPL SEMYQNIRDG
HYLEPTHLSP SARSLIARLL APDPAERPSL DHLLQDDFFS QGFTPERLPP HSCHSPPVFA
FPPPLGRLFR KVGQLLLTQC RPPCPFTSKE ASGPGEEGTE PDHMEAGNEE RDPLCTEGRI
HLLTLGTPRT GLAGPKGSLA LQLEVATRKL FLCLDAGPMA GQDPPGEQRP VLWAPKWVDY
SLKYGFGYQL SDGGSGVLFR DGSHMALRPQ GGHVSYQPDQ GTLWTFTLRD VPSPLRAKLA
VLRLFACYMQ RRLREEGTVP MPATPASPDI SLLSFIADSQ AMVMLFSNGT VQVSLKTSQT
QLVLSGEDED LLLTLQEPGG PAVGVSYTLD VLRSHGFTLA VHHHLRHGLH LLQSV
