ID   CDK20_MACMU             Reviewed;         243 AA.
AC   Q5EDC3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=Cell cycle-related kinase;
DE   AltName: Full=Cell division protein kinase 20;
DE   AltName: Full=Cyclin-dependent protein kinase H;
GN   Name=CDK20; Synonyms=CCRK, CDCH;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RA   Qiu H., Depre C.;
RT   "Macaca mulatta cardiac p42, splice variant.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: 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. Involved in cell growth. Activates CDK2, a kinase involved
CC       in the control of the cell cycle, by phosphorylating residue 'Thr-160'
CC       (By similarity). {ECO:0000250}.
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. Interacts with TBC1D32 and MAK. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Cell projection, cilium {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms may be produced.;
CC       Name=1; Synonyms=Cardiac CCRK;
CC         IsoId=Q5EDC3-1; Sequence=Displayed;
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; AY904368; AAW82350.1; -; mRNA.
DR   RefSeq; NP_001028097.1; NM_001032925.1.
DR   AlphaFoldDB; Q5EDC3; -.
DR   SMR; Q5EDC3; -.
DR   STRING; 9544.ENSMMUP00000047272; -.
DR   PaxDb; 9544-ENSMMUP00000013685; -.
DR   GeneID; 574316; -.
DR   KEGG; mcc:574316; -.
DR   CTD; 23552; -.
DR   eggNOG; KOG0659; Eukaryota.
DR   InParanoid; Q5EDC3; -.
DR   OrthoDB; 244018at2759; -.
DR   Proteomes; UP000006718; Unassembled WGS sequence.
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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   2: Evidence at transcript 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..243
FT                   /note="Cyclin-dependent kinase 20"
FT                   /id="PRO_0000085702"
FT   DOMAIN          4..243
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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"
SQ   SEQUENCE   243 AA;  27028 MW;  DB08921602FA260B CRC64;
     MDQYCILGRI GEGAHGIVFK AKHVETGEIV ALKKVALRRL EDGFPNQALR EIKALQEMGD
     NQYVVQLKAV FPHGGGFVLA FEFMLSDLAE VVRHAQRPLA QAQVKSYLQM LLKGVAFCHA
     NNIVHRDLKP ANLLISASGQ LKIADFGLAR VFSPDGSRLY THQVATRSSL SCRTTTRSPL
     RSRCPCPWRR CCLTSLPRHW ICWVNSFSTL LTSASQLPRL SSISTSSQLP CLPIHLSCRF
     LSV
//