ID CDK20_DANRE Reviewed; 344 AA. AC A8WIP6; Q5PRE2; DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 08-MAY-2019, entry version 85. DE RecName: Full=Cyclin-dependent kinase 20; DE EC=2.7.11.22; DE AltName: Full=Cell cycle-related kinase; DE AltName: Full=Cell division protein kinase 20; GN Name=cdk20; Synonyms=ccrk; ORFNames=si:dkeyp-77f7.1, zgc:101530; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=20159594; DOI=10.1016/j.devcel.2009.12.014; RA Ko H.W., Norman R.X., Tran J., Fuller K.P., Fukuda M., RA Eggenschwiler J.T.; RT "Broad-minded links cell cycle-related kinase to cilia assembly and RT hedgehog signal transduction."; RL Dev. Cell 18:237-247(2010). CC -!- FUNCTION: Involved in cell growth. Activates cdk2, a kinase CC involved in the control of the cell cycle, by phosphorylating CC residue 'Thr-160' (By similarity). Required for high-level Shh CC responses in the developing neural tube. Together with tbc1d32, CC controls the structure of the primary cilium by coordinating CC assembly of the ciliary membrane and axoneme, allowing gli2 to be CC properly activated in response to SHH signaling. {ECO:0000250, CC ECO:0000269|PubMed:20159594}. 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, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.11.22; 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=2.7.11.22; CC -!- SUBUNIT: Monomer. Interacts with tbc1d32. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm CC {ECO:0000250}. Cell projection, cilium {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Fish lacking cdk20 are viable during CC embryogenesis and early larval stages, but exhibit curvature of CC the body axis and curled cilia in distal kidney tubules. CC {ECO:0000269|PubMed:20159594}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC CC Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH86697.1; Type=Frameshift; Positions=84; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX571687; CAP19557.1; -; Genomic_DNA. DR EMBL; BC086697; AAH86697.1; ALT_FRAME; mRNA. DR RefSeq; NP_001008655.1; NM_001008655.1. DR RefSeq; XP_005166746.1; XM_005166689.3. DR STRING; 7955.ENSDARP00000113146; -. DR PaxDb; A8WIP6; -. DR PRIDE; A8WIP6; -. DR Ensembl; ENSDART00000140098; ENSDARP00000113146; ENSDARG00000003867. DR GeneID; 494112; -. DR KEGG; dre:494112; -. DR CTD; 23552; -. DR ZFIN; ZDB-GENE-041212-84; cdk20. DR eggNOG; KOG0659; Eukaryota. DR eggNOG; ENOG410XQDH; LUCA. DR GeneTree; ENSGT00940000159128; -. DR HOGENOM; HOG000233024; -. DR InParanoid; A8WIP6; -. DR KO; K08817; -. DR OMA; LHPYFFT; -. DR OrthoDB; 1367115at2759; -. DR PhylomeDB; A8WIP6; -. DR TreeFam; TF327240; -. DR PRO; PR:A8WIP6; -. DR Proteomes; UP000000437; Chromosome 8. DR Bgee; ENSDARG00000003867; Expressed in 16 organ(s), highest expression level in testis. DR ExpressionAtlas; A8WIP6; baseline. DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0070985; C:transcription factor TFIIK complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN. DR GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW. DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central. DR InterPro; IPR011009; Kinase-like_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 SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 2: Evidence at transcript level; KW ATP-binding; Cell cycle; Cell division; Cell projection; Cilium; KW Complete proteome; Cytoplasm; Developmental protein; Kinase; KW Nucleotide-binding; Nucleus; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 344 Cyclin-dependent kinase 20. FT /FTId=PRO_0000393616. FT DOMAIN 4 288 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 10 18 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 127 127 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 33 33 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. SQ SEQUENCE 344 AA; 39025 MW; D4C820FAF9C7FB62 CRC64; MDQYSILGRI GEGAHGIVFK AKHIETGETV ALKKVALRRL EDGIPNQALR EIKALQEIED NQYVVKLKDV FPHGTGFVLV FEYMLSDLSE VIRNSQRPLT ASQVKSYMMM LLKGVAFCHE NSIMHRDLKP ANLLISSTGH LKIADFGLAR LFSNEGDRLY SHQVATRWYR APELLYGARK YDEGVDLWAV GCIFGELLNN SPLFPGENDI EQLCCVLRVL GTPNQKVWPE ITELPDYNKI TFKENPPIPL EEIVPDTSPQ AVDLLKKFLV YPSKQRISAR QALLHPYFFT DPLPAHHSEL PIPQRGGKHS RQRMQPPHEF TVDRPLHESV VDPSLIQKHA MSCS //