ID CDK20_MOUSE Reviewed; 346 AA.
AC Q9JHU3; Q5EDC2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 157.
DE RecName: Full=Cyclin-dependent kinase 20;
DE EC=2.7.11.22;
DE AltName: Full=CDK-activating kinase p42;
DE Short=CAK-kinase p42;
DE AltName: Full=CDK-related protein kinase PNQLARE;
DE AltName: Full=Cell cycle-related kinase;
DE AltName: Full=Cell division protein kinase 20;
DE AltName: Full=Cyclin-dependent protein kinase H;
DE AltName: Full=Cyclin-kinase-activating kinase p42;
GN Name=Cdk20; Synonyms=Ccrk, Cdch;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129/SvJ;
RA Liao J.C., Fisher R.P.;
RT "PNQALRE a novel member of the CDK family.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Heart;
RA Qiu H., Depre C.;
RT "Mouse p42(CCRK), cardiac variant.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [4]
RP FUNCTION, INTERACTION WITH TBC1D32, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
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., 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 involved in
CC the control of the cell cycle, by phosphorylating residue 'Thr-160' (By
CC similarity). Required for high-level Shh responses in the developing
CC neural tube. Together with TBC1D32, controls the structure of the
CC primary cilium by coordinating assembly of the ciliary membrane and
CC axoneme, allowing GLI2 to be properly activated in response to SHH
CC signaling. {ECO:0000250, 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, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; 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 (By similarity). Interacts with MAK (By similarity).
CC Interacts with TBC1D32. {ECO:0000250, ECO:0000269|PubMed:20159594}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20159594}. Cytoplasm
CC {ECO:0000269|PubMed:20159594}. Cell projection, cilium
CC {ECO:0000269|PubMed:20159594}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JHU3-1; Sequence=Displayed;
CC Name=2; Synonyms=Cardiac CCRK;
CC IsoId=Q9JHU3-2; Sequence=VSP_016753, VSP_016754;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; AY005133; AAF89089.1; -; mRNA.
DR EMBL; AY904369; AAW82351.1; -; mRNA.
DR EMBL; BC031907; AAH31907.1; -; mRNA.
DR CCDS; CCDS26601.1; -. [Q9JHU3-1]
DR RefSeq; NP_444410.1; NM_053180.2. [Q9JHU3-1]
DR AlphaFoldDB; Q9JHU3; -.
DR SMR; Q9JHU3; -.
DR STRING; 10090.ENSMUSP00000021939; -.
DR iPTMnet; Q9JHU3; -.
DR PhosphoSitePlus; Q9JHU3; -.
DR jPOST; Q9JHU3; -.
DR MaxQB; Q9JHU3; -.
DR PaxDb; 10090-ENSMUSP00000021939; -.
DR ProteomicsDB; 281435; -. [Q9JHU3-1]
DR ProteomicsDB; 281436; -. [Q9JHU3-2]
DR Pumba; Q9JHU3; -.
DR Antibodypedia; 27918; 375 antibodies from 30 providers.
DR DNASU; 105278; -.
DR Ensembl; ENSMUST00000021939.8; ENSMUSP00000021939.7; ENSMUSG00000021483.9. [Q9JHU3-1]
DR GeneID; 105278; -.
DR KEGG; mmu:105278; -.
DR UCSC; uc007qyx.1; mouse. [Q9JHU3-1]
DR AGR; MGI:2145349; -.
DR CTD; 23552; -.
DR MGI; MGI:2145349; Cdk20.
DR VEuPathDB; HostDB:ENSMUSG00000021483; -.
DR eggNOG; KOG0659; Eukaryota.
DR GeneTree; ENSGT00940000159128; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q9JHU3; -.
DR OMA; KITFPYH; -.
DR OrthoDB; 244018at2759; -.
DR PhylomeDB; Q9JHU3; -.
DR TreeFam; TF327240; -.
DR BRENDA; 2.7.11.22; 3474.
DR BioGRID-ORCS; 105278; 3 hits in 81 CRISPR screens.
DR ChiTaRS; Cdk20; mouse.
DR PRO; PR:Q9JHU3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JHU3; Protein.
DR Bgee; ENSMUSG00000021483; Expressed in primary oocyte and 123 other cell types or tissues.
DR ExpressionAtlas; Q9JHU3; baseline and differential.
DR Genevisible; Q9JHU3; MM.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990403; P:embryonic brain development; IMP:MGI.
DR GO; GO:0031076; P:embryonic camera-type eye development; IMP:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; IMP:MGI.
DR GO; GO:0021508; P:floor plate formation; IMP:MGI.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR GO; GO:1903317; P:regulation of protein maturation; IMP:MGI.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IGI:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR CDD; cd07832; STKc_CCRK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR048002; CDK20-like_STKc.
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 PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR PANTHER; PTHR24056:SF171; CYCLIN-DEPENDENT KINASE 20; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell projection; Cilium; Cytoplasm; Developmental protein; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..346
FT /note="Cyclin-dependent kinase 20"
FT /id="PRO_0000085703"
FT DOMAIN 4..288
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 298..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 168..243
FT /note="WYRAPELLYGARQYDQGVDLWAVGCIMGELLNGSPLFPGENDIEQLCCVLRI
FT LGTPSPRVWPEITELPDYNKISFK -> SSLSCRTTTRSPLRSRCPCPWRRCCLTSLPR
FT HWICWVNSFSTLLTSASQLPRLSSISTSSQLPCLPIHLSCRFLSV (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016753"
FT VAR_SEQ 244..346
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016754"
FT CONFLICT 44
FT /note="I -> F (in Ref. 2; AAW82351)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="I -> M (in Ref. 2; AAW82351)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="S -> N (in Ref. 2; AAW82351)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="A -> G (in Ref. 2; AAW82351)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="P -> Q (in Ref. 2; AAW82351)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="G -> S (in Ref. 2; AAW82351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 38379 MW; ACCACE0C3FC4B833 CRC64;
MDQYCILGRI GEGAHGIVFK AKHVETGEIV ALKKVALRRL EDGIPNQALR EIKALQEIED
SQYVVQLKAV FPHGAGFVLA FEFMLSDLAE VVRHAQRPLA PAQVKSYLQM LLKGVAFCHA
NNIVHRDLKP ANLLISASGQ LKIADFGLAR VFSPDGGRLY THQVATRWYR APELLYGARQ
YDQGVDLWAV GCIMGELLNG SPLFPGENDI EQLCCVLRIL GTPSPRVWPE ITELPDYNKI
SFKEQAPVPL EEVLPDASPQ ALDLLGQFLL YPPRQRIAAS QALLHQYFFT APLPAHPSEL
PIPQRPGGPA PKAHPGPPHV HDFHVDRPLE ESLLNPELIR PFIPEG
//
