CDK20_RAT
ID CDK20_RAT Reviewed; 346 AA.
AC Q4KM34;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 119.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH98838.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; BC098838; AAH98838.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001020923.2; NM_001025752.2.
DR AlphaFoldDB; Q4KM34; -.
DR SMR; Q4KM34; -.
DR STRING; 10116.ENSRNOP00000024466; -.
DR jPOST; Q4KM34; -.
DR PaxDb; Q4KM34; -.
DR Ensembl; ENSRNOT00000024466; ENSRNOP00000024466; ENSRNOG00000017991.
DR GeneID; 364666; -.
DR KEGG; rno:364666; -.
DR UCSC; RGD:1305219; rat.
DR CTD; 23552; -.
DR RGD; 1305219; Cdk20.
DR eggNOG; KOG0659; Eukaryota.
DR GeneTree; ENSGT00940000159128; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q4KM34; -.
DR OMA; RWEDIFP; -.
DR OrthoDB; 1367115at2759; -.
DR PhylomeDB; Q4KM34; -.
DR TreeFam; TF327240; -.
DR PRO; PR:Q4KM34; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000017991; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q4KM34; RN.
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; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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; ISO:RGD.
DR GO; GO:0031076; P:embryonic camera-type eye development; ISO:RGD.
DR GO; GO:0048706; P:embryonic skeletal system development; ISO:RGD.
DR GO; GO:0021508; P:floor plate formation; ISO:RGD.
DR GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; ISO:RGD.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR GO; GO:0061512; P:protein localization to cilium; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:1903317; P:regulation of protein maturation; ISO:RGD.
DR GO; GO:1901620; P:regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; ISO:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
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; Cytoplasm;
KW Developmental protein; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..346
FT /note="Cyclin-dependent kinase 20"
FT /id="PRO_0000085705"
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"
SQ SEQUENCE 346 AA; 38449 MW; E4D34F943BEA6350 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 EEVLPDASHQ ALDLLGQFLL YPPRQRIAAS QALLHQYFFT APLPAHPSEL
PIPQRPGGPT PKAHPGPPHV HDFHVDRPLE ESLLNPELIR PFIPEG
