CDK10_BOVIN
ID CDK10_BOVIN Reviewed; 361 AA.
AC Q2TBL8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cyclin-dependent kinase 10;
DE EC=2.7.11.22;
DE AltName: Full=Cell division protein kinase 10;
GN Name=CDK10;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cyclin-dependent kinase that phosphorylates the transcription
CC factor ETS2 (in vitro) and positively controls its proteasomal
CC degradation (in cells). Involved in the regulation of actin
CC cytoskeleton organization through the phosphorylation of actin dynamics
CC regulators such as PKN2. Is a negative regulator of ciliogenesis
CC through phosphorylation of PKN2 and promotion of RhoA signaling.
CC {ECO:0000250|UniProtKB:Q15131}.
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: Heterodimer with CCNQ, the interaction is required for kinase
CC activity. Interacts with ETS2. Interacts with PRK2.
CC {ECO:0000250|UniProtKB:Q15131}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q15131}.
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; BC109954; AAI09955.1; -; mRNA.
DR RefSeq; NP_001033666.1; NM_001038577.2.
DR AlphaFoldDB; Q2TBL8; -.
DR SMR; Q2TBL8; -.
DR STRING; 9913.ENSBTAP00000044609; -.
DR PaxDb; Q2TBL8; -.
DR PRIDE; Q2TBL8; -.
DR Ensembl; ENSBTAT00000047400; ENSBTAP00000044609; ENSBTAG00000033333.
DR GeneID; 615171; -.
DR KEGG; bta:615171; -.
DR CTD; 8558; -.
DR VEuPathDB; HostDB:ENSBTAG00000033333; -.
DR VGNC; VGNC:27116; CDK10.
DR eggNOG; KOG0663; Eukaryota.
DR GeneTree; ENSGT00940000158102; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q2TBL8; -.
DR OMA; TWPGFRS; -.
DR OrthoDB; 925637at2759; -.
DR TreeFam; TF101026; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000033333; Expressed in retina and 106 other tissues.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR CDD; cd07845; STKc_CDK10; 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 InterPro; IPR044093; STKc_CDK10.
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 projection; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..361
FT /note="Cyclin-dependent kinase 10"
FT /id="PRO_0000261032"
FT DOMAIN 37..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 332..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 43..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15131"
SQ SEQUENCE 361 AA; 41047 MW; 166CEE224496DEE8 CRC64;
MGEPEPEQIR LKCVRKEGFF TVPPEHRLGR CRSVKEFEKL NRIGEGTYGI VYRARDTHTD
EIVALKKVRM DKEKDGVPIS SLREITLLLR LRHPNIVELK EVVVGNHLES IFLVMGYCEQ
DLASLLENMP TPFSEAQVKC IVLQVLRGLQ YLHRNFIIHR DLKVSNLLMT DKGCVKTADF
GLARAYGIPV KPMTPKVVTL WYRAPELLLG TTTQTTSIDM WAVGCILAEL LAHKPLLPGT
SEIHQVDLIV QLLGTPSENI WPGFSQLPLA SQYSLRKQPY NNLKHKFPWL SEAGLRLMNL
LFMYDPKKRA TAGDCLESSY FKEKPLPCEP ELMPTFPHHR NKRATPATSL GTESQSRRGR
P
