CDK10_HUMAN
ID CDK10_HUMAN Reviewed; 360 AA.
AC Q15131; A8K370; A8K8I6; A8MXU6; B3KQJ3; B7Z420; D3DX82; D3DX83; Q0VGZ7;
AC Q15130; Q6PJC0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Cyclin-dependent kinase 10;
DE EC=2.7.11.22;
DE AltName: Full=Cell division protein kinase 10;
DE AltName: Full=Serine/threonine-protein kinase PISSLRE;
GN Name=CDK10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=8208557;
RA Grana X., Claudio P.P., De Luca A., Sang N., Giordano A.;
RT "PISSLRE, a human novel CDC2-related protein kinase.";
RL Oncogene 9:2097-2103(1994).
RN [2]
RP SEQUENCE REVISION.
RA Grana X., Claudio P.P., De Luca A., Sang N., Giordano A.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8084611;
RA Brambilla R., Draetta G.;
RT "Molecular cloning of PISSLRE, a novel putative member of the cdk family of
RT protein serine/threonine kinases.";
RL Oncogene 9:3037-3041(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10036189; DOI=10.1006/geno.1998.5676;
RA Crawford J., Ianzano L., Savino M., Whitmore S., Cleton-Jansen A.-M.,
RA Settasatiani C., D'Apolito M., Seshadri R., Pronk J.C., Auerbach A.D.,
RA Verlander P.C., Mathew C.G., Tipping A.J., Doggett N.A., Zelante L.,
RA Callen D.F., Savoia A.;
RT "The PISSLRE gene: structure, exon skipping, and exclusion as tumor
RT suppressor in breast cancer.";
RL Genomics 56:90-97(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5; 6 AND 7).
RC TISSUE=Brain, Colon, Ovary, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Bechtel S., Schupp I., Duda A., Wellenreuther R., Mehrle A., Ruschke V.,
RA Poustka A., Wiemann S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Colon, and Lung;
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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH CCNQ.
RX PubMed=24218572; DOI=10.1073/pnas.1306814110;
RA Guen V.J., Gamble C., Flajolet M., Unger S., Thollet A., Ferandin Y.,
RA Superti-Furga A., Cohen P.A., Meijer L., Colas P.;
RT "CDK10/cyclin M is a protein kinase that controls ETS2 degradation and is
RT deficient in STAR syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19525-19530(2013).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRK2.
RX PubMed=27104747; DOI=10.1080/15384101.2016.1147632;
RA Guen V.J., Gamble C., Perez D.E., Bourassa S., Zappel H., Gaertner J.,
RA Lees J.A., Colas P.;
RT "STAR syndrome-associated CDK10/Cyclin M regulates actin network
RT architecture and ciliogenesis.";
RL Cell Cycle 15:678-688(2016).
RN [14]
RP INVOLVEMENT IN ALKAS.
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).
RN [15]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-96; SER-168; HIS-342 AND TYR-358.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Cyclin-dependent kinase that phosphorylates the transcription
CC factor ETS2 (in vitro) and positively controls its proteasomal
CC degradation (in cells) (PubMed:24218572). Involved in the regulation of
CC actin cytoskeleton organization through the phosphorylation of actin
CC dynamics regulators such as PKN2. Is a negative regulator of
CC ciliogenesis through phosphorylation of PKN2 and promotion of RhoA
CC signaling (PubMed:27104747). {ECO:0000269|PubMed:24218572,
CC ECO:0000269|PubMed:27104747}.
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 Evidence={ECO:0000269|PubMed:24218572};
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; Evidence={ECO:0000269|PubMed:24218572};
CC -!- SUBUNIT: Heterodimer with CCNQ, the interaction is required for kinase
CC activity. Interacts with ETS2. Interacts with PRK2 (PubMed:27104747).
CC {ECO:0000269|PubMed:24218572, ECO:0000269|PubMed:27104747}.
CC -!- INTERACTION:
CC Q15131; P15036: ETS2; NbExp=2; IntAct=EBI-1646959, EBI-1646991;
CC Q15131; P08238: HSP90AB1; NbExp=3; IntAct=EBI-1646959, EBI-352572;
CC Q15131; Q13526: PIN1; NbExp=5; IntAct=EBI-1646959, EBI-714158;
CC Q15131-1; Q8N1B3: CCNQ; NbExp=7; IntAct=EBI-11507283, EBI-3925043;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:27104747}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q15131-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15131-2; Sequence=VSP_021642;
CC Name=3;
CC IsoId=Q15131-3; Sequence=VSP_021642, VSP_021643;
CC Name=4;
CC IsoId=Q15131-4; Sequence=VSP_021642, VSP_021644;
CC Name=5;
CC IsoId=Q15131-5; Sequence=VSP_054969, VSP_054972, VSP_054973;
CC Name=6;
CC IsoId=Q15131-6; Sequence=VSP_054969, VSP_054970, VSP_054971;
CC Name=7;
CC IsoId=Q15131-7; Sequence=VSP_021642, VSP_054972;
CC -!- DISEASE: Al Kaissi syndrome (ALKAS) [MIM:617694]: An autosomal
CC recessive developmental disorder characterized by growth retardation,
CC spine malformation, facial dysmorphisms, and developmental delay.
CC {ECO:0000269|PubMed:28886341}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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; L33264; AAA60092.2; -; mRNA.
DR EMBL; X78342; CAA55137.1; -; mRNA.
DR EMBL; AJ010341; CAB37619.1; -; Genomic_DNA.
DR EMBL; AJ010342; CAB37619.1; JOINED; Genomic_DNA.
DR EMBL; AJ010343; CAB37619.1; JOINED; Genomic_DNA.
DR EMBL; AJ010344; CAB37619.1; JOINED; Genomic_DNA.
DR EMBL; AM392903; CAL37781.1; -; mRNA.
DR EMBL; AK075036; BAG52055.1; -; mRNA.
DR EMBL; AK290485; BAF83174.1; -; mRNA.
DR EMBL; AK292351; BAF85040.1; -; mRNA.
DR EMBL; AK296631; BAH12406.1; -; mRNA.
DR EMBL; AM393177; CAL38055.1; -; mRNA.
DR EMBL; AM393204; CAL38082.1; -; mRNA.
DR EMBL; AC010538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471184; EAW66701.1; -; Genomic_DNA.
DR EMBL; CH471184; EAW66703.1; -; Genomic_DNA.
DR EMBL; CH471184; EAW66704.1; -; Genomic_DNA.
DR EMBL; CH471184; EAW66705.1; -; Genomic_DNA.
DR EMBL; CH471184; EAW66706.1; -; Genomic_DNA.
DR EMBL; CH471184; EAW66707.1; -; Genomic_DNA.
DR EMBL; CH471184; EAW66708.1; -; Genomic_DNA.
DR EMBL; CH471184; EAW66710.1; -; Genomic_DNA.
DR EMBL; BC017342; AAH17342.1; -; mRNA.
DR EMBL; BC025301; AAH25301.1; -; mRNA.
DR CCDS; CCDS10984.2; -. [Q15131-1]
DR CCDS; CCDS32514.2; -. [Q15131-4]
DR PIR; S49330; S49330.
DR RefSeq; NP_001092003.2; NM_001098533.2. [Q15131-3]
DR RefSeq; NP_001153839.1; NM_001160367.1. [Q15131-2]
DR RefSeq; NP_443713.2; NM_052987.3. [Q15131-4]
DR RefSeq; NP_443714.3; NM_052988.4. [Q15131-1]
DR RefSeq; XP_016879297.1; XM_017023808.1. [Q15131-2]
DR RefSeq; XP_016879298.1; XM_017023809.1. [Q15131-3]
DR RefSeq; XP_016879299.1; XM_017023810.1. [Q15131-4]
DR AlphaFoldDB; Q15131; -.
DR SMR; Q15131; -.
DR BioGRID; 114128; 21.
DR ComplexPortal; CPX-326; Cyclin M-CDK10 complex. [Q15131-1]
DR IntAct; Q15131; 32.
DR MINT; Q15131; -.
DR STRING; 9606.ENSP00000338673; -.
DR BindingDB; Q15131; -.
DR ChEMBL; CHEMBL1795191; -.
DR iPTMnet; Q15131; -.
DR PhosphoSitePlus; Q15131; -.
DR BioMuta; CDK10; -.
DR DMDM; 6226784; -.
DR EPD; Q15131; -.
DR jPOST; Q15131; -.
DR MassIVE; Q15131; -.
DR MaxQB; Q15131; -.
DR PaxDb; Q15131; -.
DR PeptideAtlas; Q15131; -.
DR PRIDE; Q15131; -.
DR ProteomicsDB; 60454; -. [Q15131-1]
DR ProteomicsDB; 60455; -. [Q15131-2]
DR ProteomicsDB; 60456; -. [Q15131-3]
DR ProteomicsDB; 60457; -. [Q15131-4]
DR Antibodypedia; 30892; 327 antibodies from 35 providers.
DR DNASU; 8558; -.
DR Ensembl; ENST00000353379.12; ENSP00000338673.7; ENSG00000185324.22. [Q15131-1]
DR Ensembl; ENST00000505473.5; ENSP00000424415.1; ENSG00000185324.22. [Q15131-4]
DR Ensembl; ENST00000617879.1; ENSP00000484357.1; ENSG00000185324.22. [Q15131-4]
DR GeneID; 8558; -.
DR KEGG; hsa:8558; -.
DR MANE-Select; ENST00000353379.12; ENSP00000338673.7; NM_052988.5; NP_443714.3.
DR UCSC; uc002fod.4; human. [Q15131-1]
DR CTD; 8558; -.
DR DisGeNET; 8558; -.
DR GeneCards; CDK10; -.
DR HGNC; HGNC:1770; CDK10.
DR HPA; ENSG00000185324; Low tissue specificity.
DR MalaCards; CDK10; -.
DR MIM; 603464; gene.
DR MIM; 617694; phenotype.
DR neXtProt; NX_Q15131; -.
DR OpenTargets; ENSG00000185324; -.
DR PharmGKB; PA26307; -.
DR VEuPathDB; HostDB:ENSG00000185324; -.
DR eggNOG; KOG0663; Eukaryota.
DR GeneTree; ENSGT00940000158102; -.
DR InParanoid; Q15131; -.
DR OMA; TWPGFRS; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; Q15131; -.
DR TreeFam; TF101026; -.
DR BRENDA; 2.7.11.22; 2681.
DR PathwayCommons; Q15131; -.
DR SignaLink; Q15131; -.
DR SIGNOR; Q15131; -.
DR BioGRID-ORCS; 8558; 42 hits in 1120 CRISPR screens.
DR ChiTaRS; CDK10; human.
DR GeneWiki; Cyclin-dependent_kinase_10; -.
DR GenomeRNAi; 8558; -.
DR Pharos; Q15131; Tchem.
DR PRO; PR:Q15131; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q15131; protein.
DR Bgee; ENSG00000185324; Expressed in right uterine tube and 196 other tissues.
DR ExpressionAtlas; Q15131; baseline and differential.
DR Genevisible; Q15131; HS.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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; IDA:UniProtKB.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA: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; IMP:UniProtKB.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IDA:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; TAS:ProtInc.
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 Alternative splicing; ATP-binding; Cell projection;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..360
FT /note="Cyclin-dependent kinase 10"
FT /id="PRO_0000085809"
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:18669648,
FT ECO:0007744|PubMed:18691976"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8208557,
FT ECO:0000303|Ref.6"
FT /id="VSP_021642"
FT VAR_SEQ 48..54
FT /note="GTYGIVY -> D (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054969"
FT VAR_SEQ 141..160
FT /note="KCIVLQVLRGLQYLHRNFII -> RGRGAWGGGMGFMGPCGAHL (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054970"
FT VAR_SEQ 161..360
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054971"
FT VAR_SEQ 180..194
FT /note="ADFGLARAYGVPVKP -> GGCNLGQALSLDGTW (in isoform 5 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054972"
FT VAR_SEQ 195..360
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054973"
FT VAR_SEQ 306..311
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT /id="VSP_021643"
FT VAR_SEQ 329..360
FT /note="PCEPELMPTFPHHRNKRAAPATSEGQSKRCKP -> RLPISGVCEGCREPG
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8208557"
FT /id="VSP_021644"
FT VARIANT 96
FT /note="P -> L (in dbSNP:rs55819627)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041983"
FT VARIANT 168
FT /note="N -> S (in dbSNP:rs56340740)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041984"
FT VARIANT 342
FT /note="R -> H (in dbSNP:rs55757604)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041985"
FT VARIANT 358
FT /note="C -> Y (in dbSNP:rs56242003)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041986"
SQ SEQUENCE 360 AA; 41038 MW; 25B28560961103F4 CRC64;
MAEPDLECEQ IRLKCIRKEG FFTVPPEHRL GRCRSVKEFE KLNRIGEGTY GIVYRARDTQ
TDEIVALKKV RMDKEKDGIP ISSLREITLL LRLRHPNIVE LKEVVVGNHL ESIFLVMGYC
EQDLASLLEN MPTPFSEAQV KCIVLQVLRG LQYLHRNFII HRDLKVSNLL MTDKGCVKTA
DFGLARAYGV PVKPMTPKVV TLWYRAPELL LGTTTQTTSI DMWAVGCILA ELLAHRPLLP
GTSEIHQIDL IVQLLGTPSE NIWPGFSKLP LVGQYSLRKQ PYNNLKHKFP WLSEAGLRLL
HFLFMYDPKK RATAGDCLES SYFKEKPLPC EPELMPTFPH HRNKRAAPAT SEGQSKRCKP
