PLK5_HUMAN
ID PLK5_HUMAN Reviewed; 336 AA.
AC Q496M5; B3KNR4; Q1ZYM0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Inactive serine/threonine-protein kinase PLK5;
DE AltName: Full=Polo-like kinase 5;
DE Short=PLK-5;
GN Name=PLK5; Synonyms=PLK5P; ORFNames=FG060302;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Liang M., Tang Z.,
RA Huang B., Lin L., Yang S.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 [5]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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:21245385}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:21245385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q496M5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q496M5-2; Sequence=VSP_023654;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, neurons and glial cells.
CC Also expressed in highly differentiated cells, such as the serous acini
CC in the parotid gland, distal and proximal tubules of the kidney,
CC tubules of the seminal gland, Kupffer cells and some hepatocytes in the
CC liver, and some cells in the germinal center of lymph nodes (at protein
CC level). {ECO:0000269|PubMed:21245385}.
CC -!- INDUCTION: Down-regulated in primary brain tumors.
CC {ECO:0000269|PubMed:21245385}.
CC -!- DOMAIN: The truncated protein kinase domain is predicted to be
CC catalytically inactive; has lost the main activatory
CC autophosphorylation site and the conserved key residues involved in
CC phospho-substrate. The C-terminal region (containing the POLO box
CC domain) is sufficient for inducing cell cycle arrest.
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; AK054808; BAG51426.1; -; mRNA.
DR EMBL; DQ424898; ABD83663.1; -; mRNA.
DR EMBL; AC027307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100791; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS59328.1; -. [Q496M5-1]
DR RefSeq; NP_001230008.1; NM_001243079.1. [Q496M5-1]
DR AlphaFoldDB; Q496M5; -.
DR SMR; Q496M5; -.
DR STRING; 9606.ENSP00000466248; -.
DR PhosphoSitePlus; Q496M5; -.
DR BioMuta; PLK5; -.
DR DMDM; 308153664; -.
DR PaxDb; Q496M5; -.
DR PeptideAtlas; Q496M5; -.
DR PRIDE; Q496M5; -.
DR Antibodypedia; 64895; 182 antibodies from 29 providers.
DR DNASU; 126520; -.
DR Ensembl; ENST00000334770.9; ENSP00000466248.1; ENSG00000185988.15. [Q496M5-1]
DR Ensembl; ENST00000454744.7; ENSP00000468376.1; ENSG00000185988.15. [Q496M5-1]
DR Ensembl; ENST00000588430.3; ENSP00000465896.2; ENSG00000185988.15. [Q496M5-2]
DR Ensembl; ENST00000673796.1; ENSP00000501198.1; ENSG00000185988.15. [Q496M5-1]
DR Ensembl; ENST00000673896.1; ENSP00000501063.1; ENSG00000185988.15. [Q496M5-2]
DR GeneID; 126520; -.
DR KEGG; hsa:126520; -.
DR MANE-Select; ENST00000454744.7; ENSP00000468376.1; NM_001243079.2; NP_001230008.1.
DR UCSC; uc002ltf.4; human. [Q496M5-1]
DR CTD; 126520; -.
DR DisGeNET; 126520; -.
DR GeneCards; PLK5; -.
DR HGNC; HGNC:27001; PLK5.
DR HPA; ENSG00000185988; Tissue enhanced (brain, cervix, testis).
DR neXtProt; NX_Q496M5; -.
DR OpenTargets; ENSG00000185988; -.
DR VEuPathDB; HostDB:ENSG00000185988; -.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000162321; -.
DR HOGENOM; CLU_830408_0_0_1; -.
DR InParanoid; Q496M5; -.
DR OMA; SAGWHPH; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; Q496M5; -.
DR PathwayCommons; Q496M5; -.
DR BioGRID-ORCS; 126520; 10 hits in 1057 CRISPR screens.
DR ChiTaRS; PLK5; human.
DR GenomeRNAi; 126520; -.
DR Pharos; Q496M5; Tbio.
DR PRO; PR:Q496M5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q496M5; protein.
DR Bgee; ENSG00000185988; Expressed in right hemisphere of cerebellum and 90 other tissues.
DR ExpressionAtlas; Q496M5; baseline and differential.
DR Genevisible; Q496M5; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IBA:GO_Central.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
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: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; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Differentiation; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..336
FT /note="Inactive serine/threonine-protein kinase PLK5"
FT /id="PRO_0000280397"
FT DOMAIN 1..65
FT /note="Protein kinase; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 259..334
FT /note="POLO box"
FT REGION 109..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 239..275
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_023654"
FT CONFLICT 314
FT /note="R -> Q (in Ref. 1; BAG51426 and 4; BC100791)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="Missing (in Ref. 2; ABD83663)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="G -> R (in Ref. 2; ABD83663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 36329 MW; 782A33DF18A7E445 CRC64;
MYTVLTGTPP FMASPLSEMY QNIREGHYPE PAHLSANARR LIVHLLAPNP AERPSLDHLL
QDDFFTQGFT PDRLPAHSCH SPPIFAIPPP LGRIFRKVGQ RLLTQCRPPC PFTPKEASGP
GEGGPDPDSM EWDGESSLSA KEVPCLEGPI HLVAQGTLQS DLAGPEGSRR PEVEAALRHL
QLCLDVGPPA TQDPLGEQQP ILWAPKWVDY SSKYGFGYQL LDGGRTGRHP HGPATPRREG
TLPTPVPPAG PGLCLLRFLA SEHALLLLFS NGMVQVSFSG VPAQLVLSGE GEGLQLTLWE
QGSPGTSYSL DVPRSHGCAP TTGQHLHHAL RMLQSI
