CDK10_MOUSE
ID CDK10_MOUSE Reviewed; 360 AA.
AC Q3UMM4; Q3UZD2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
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 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].
RX PubMed=16741970; DOI=10.1002/jcb.20981;
RA Bagella L., Giacinti C., Simone C., Giordano A.;
RT "Identification of murine cdk10: association with Ets2 transcription factor
RT and effects on the cell cycle.";
RL J. Cell. Biochem. 99:978-985(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=28886341; DOI=10.1016/j.ajhg.2017.08.003;
RA Windpassinger C., Piard J., Bonnard C., Alfadhel M., Lim S., Bisteau X.,
RA Blouin S., Ali N.B., Ng A.Y.J., Lu H., Tohari S., Talib S.Z.A., van Hul N.,
RA Caldez M.J., Van Maldergem L., Yigit G., Kayserili H., Youssef S.A.,
RA Coppola V., de Bruin A., Tessarollo L., Choi H., Rupp V., Roetzer K.,
RA Roschger P., Klaushofer K., Altmueller J., Roy S., Venkatesh B., Ganger R.,
RA Grill F., Ben Chehida F., Wollnik B., Altunoglu U., Al Kaissi A.,
RA Reversade B., Kaldis P.;
RT "CDK10 mutations in humans and mice cause severe growth retardation, spine
RT malformations, and developmental delays.";
RL Am. J. Hum. Genet. 101:391-403(2017).
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 -!- DISRUPTION PHENOTYPE: CDK10 knockout results in partial prenatal
CC lethality. Surviving mice display severe growth retardation, a reduced
CC volume of mineralized matrix in the head, femur, tibia and fibula,
CC bifidity or clefting of C1 (atlas) or C2 (axis), and absence of the
CC dens. Additional defects are present in the kidney, lung, heart,
CC spleen, liver, and muscle. At cellular level, CDK10 knockout does not
CC affect cell proliferation. However, knocked-out mouse embryonic
CC fibroblasts (MEFs) develop longer cilia. {ECO:0000269|PubMed:28886341}.
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; DQ288857; ABB96224.1; -; mRNA.
DR EMBL; AK133918; BAE21925.1; -; mRNA.
DR EMBL; AK144801; BAE26074.1; -; mRNA.
DR CCDS; CCDS22751.1; -.
DR RefSeq; NP_919426.2; NM_194444.2.
DR RefSeq; NP_919428.1; NM_194446.2.
DR AlphaFoldDB; Q3UMM4; -.
DR SMR; Q3UMM4; -.
DR BioGRID; 231589; 1.
DR ComplexPortal; CPX-327; Cyclin M-CDK10 complex.
DR STRING; 10090.ENSMUSP00000045527; -.
DR iPTMnet; Q3UMM4; -.
DR PhosphoSitePlus; Q3UMM4; -.
DR EPD; Q3UMM4; -.
DR jPOST; Q3UMM4; -.
DR MaxQB; Q3UMM4; -.
DR PaxDb; Q3UMM4; -.
DR PRIDE; Q3UMM4; -.
DR ProteomicsDB; 280037; -.
DR Antibodypedia; 30892; 327 antibodies from 35 providers.
DR DNASU; 234854; -.
DR Ensembl; ENSMUST00000036880; ENSMUSP00000045527; ENSMUSG00000033862.
DR GeneID; 234854; -.
DR KEGG; mmu:234854; -.
DR UCSC; uc009nun.2; mouse.
DR CTD; 8558; -.
DR MGI; MGI:2448549; Cdk10.
DR VEuPathDB; HostDB:ENSMUSG00000033862; -.
DR eggNOG; KOG0663; Eukaryota.
DR GeneTree; ENSGT00940000158102; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q3UMM4; -.
DR OMA; TWPGFRS; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; Q3UMM4; -.
DR TreeFam; TF101026; -.
DR BioGRID-ORCS; 234854; 6 hits in 77 CRISPR screens.
DR ChiTaRS; Cdk10; mouse.
DR PRO; PR:Q3UMM4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3UMM4; protein.
DR Bgee; ENSMUSG00000033862; Expressed in ear vesicle and 213 other tissues.
DR ExpressionAtlas; Q3UMM4; baseline and differential.
DR Genevisible; Q3UMM4; MM.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0097472; F:cyclin-dependent protein kinase activity; IGI:MGI.
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; IGI:MGI.
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:1902749; P:regulation of cell cycle G2/M phase transition; ISO:MGI.
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 1: Evidence at protein 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..360
FT /note="Cyclin-dependent kinase 10"
FT /id="PRO_0000261028"
FT DOMAIN 39..323
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 334..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 360 AA; 40961 MW; 9621FDB86E231E93 CRC64;
MAEVDLESDQ IRLKCIRKEG FFTVPPEHRL GRCRSVKEFE KLNRIGEGTY GIVYRARDTQ
TDEIVALKKV RMDKEKDGIP ISSLREITLL LRLRHPNIVE LKEVVVGNHL ESIFLVMGYC
EQDLASLLEN MPTPFSEAQV KCIMLQVLRG LQYLHRNFII HRDLKVSNLL MTDKGCVKTA
DFGLARAYGV PVKPMTPKVV TLWYRAPELL LGTTTQTTSI DMWAVGCILA ELLAHKPLLP
GTSEIHQIDL IVQLLGTPSE NIWPGFSKLP LAGQYSLRKQ PYNNLKHKFP WLSEAGLRLL
NFLFMYDPKK RATSGDCLES SYFKEKPLPC EPELMPTFPH HRNKRAAPAA AEGQSKRCRP
