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   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.
DR   Genevisible; Q9JHU3; MM.
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
//