CDK10_RAT
ID CDK10_RAT Reviewed; 358 AA.
AC Q4KM47;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 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: 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; BC098804; AAH98804.1; -; mRNA.
DR RefSeq; NP_001020893.2; NM_001025722.2.
DR RefSeq; NP_001103406.1; NM_001109936.1.
DR RefSeq; NP_001103407.1; NM_001109937.1.
DR AlphaFoldDB; Q4KM47; -.
DR SMR; Q4KM47; -.
DR STRING; 10116.ENSRNOP00000059465; -.
DR iPTMnet; Q4KM47; -.
DR PhosphoSitePlus; Q4KM47; -.
DR PaxDb; Q4KM47; -.
DR PRIDE; Q4KM47; -.
DR GeneID; 361434; -.
DR KEGG; rno:361434; -.
DR UCSC; RGD:1304851; rat.
DR CTD; 8558; -.
DR RGD; 1304851; Cdk10.
DR eggNOG; KOG0663; Eukaryota.
DR InParanoid; Q4KM47; -.
DR PhylomeDB; Q4KM47; -.
DR PRO; PR:Q4KM47; -.
DR Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0097472; F:cyclin-dependent protein kinase activity; ISO:RGD.
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; ISO:RGD.
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..358
FT /note="Cyclin-dependent kinase 10"
FT /id="PRO_0000261029"
FT DOMAIN 37..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 332..358
FT /note="Disordered"
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 358 AA; 40634 MW; F10590B86C4D4782 CRC64;
MSQCQIWVRH HLCCSFQIPT LAASLFQLGR CRSVKEFEKL NRIGEGTYGI VYRARDTQTD
EIVALKKVRM DKEKDGIPIS SLREITLLLR LRHPNIVELK EVVVGNHLES IFLVMGYCEQ
DLASLLENMP TPFSEAQVKC ILLQVLRGLQ YLHRSFIIHR DLKVSNLLMT DKGCVKTADF
GLARAYGVPV KPMTPKVVTL WYRAPELLLG TTTQTTSIDM WAVGCILAEL LAHKPLLPGT
SEIHQIDLIV QLLGTPSENI WPGFSKLPLA GQYSLRKQPY NNLKHKFPWL SEAGLRLLNF
LFMYDPKKRA TAGDCLESSY FKEKPLPCEP ELMPTFPHHR NKRAAPAATE GQSKRCRP
