CDK14_HUMAN
ID CDK14_HUMAN Reviewed; 469 AA.
AC O94921; A4D1E6; A6NK51; A8WFP6; B4DHG5; B4DNM2; Q75N06; Q75N22; Q8N764;
AC Q9H3D7; Q9UDR0;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Cyclin-dependent kinase 14;
DE EC=2.7.11.22;
DE AltName: Full=Cell division protein kinase 14;
DE AltName: Full=Serine/threonine-protein kinase PFTAIRE-1;
DE Short=hPFTAIRE1;
GN Name=CDK14; Synonyms=KIAA0834, PFTK1;
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 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=11313143; DOI=10.1016/s0378-1119(01)00391-2;
RA Yang T., Chen J.-Y.;
RT "Identification and cellular localization of human PFTAIRE1.";
RL Gene 267:165-172(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain, and Testis;
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 [8]
RP INTERACTION WITH SEPT8.
RX PubMed=12098780;
RA Yang T., Gao Y.K., Chen J.Y.;
RT "KIAA0202, a human septin family member, interacting with hPFTAIRE1.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:520-525(2002).
RN [9]
RP INTERACTION WITH YWHAB; YWHAE; YWHAH AND YWHAQ.
RX PubMed=16775625; DOI=10.1038/sj.cr.7310071;
RA Gao Y., Jiang M., Yang T., Ni J., Chen J.;
RT "A Cdc2-related protein kinase hPFTAIRE1 from human brain interacting with
RT 14-3-3 proteins.";
RL Cell Res. 16:539-547(2006).
RN [10]
RP FUNCTION.
RX PubMed=16461467; DOI=10.1073/pnas.0507660103;
RA Tang X., Guilherme A., Chakladar A., Powelka A.M., Konda S.,
RA Virbasius J.V., Nicoloro S.M., Straubhaar J., Czech M.P.;
RT "An RNA interference-based screen identifies MAP4K4/NIK as a negative
RT regulator of PPARgamma, adipogenesis, and insulin-responsive hexose
RT transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2087-2092(2006).
RN [11]
RP FUNCTION, INTERACTION WITH CCDN3 AND CDKN1A, AND MUTAGENESIS OF LYS-164.
RX PubMed=17517622; DOI=10.1073/pnas.0703327104;
RA Shu F., Lv S., Qin Y., Ma X., Wang X., Peng X., Luo Y., Xu B.E., Sun X.,
RA Wu J.;
RT "Functional characterization of human PFTK1 as a cyclin-dependent kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9248-9253(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, 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 [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCNY.
RX PubMed=20059949; DOI=10.1016/j.devcel.2009.11.006;
RA Davidson G., Shen J., Huang Y.L., Su Y., Karaulanov E., Bartscherer K.,
RA Hassler C., Stannek P., Boutros M., Niehrs C.;
RT "Cell cycle control of wnt receptor activation.";
RL Dev. Cell 17:788-799(2009).
RN [14]
RP FUNCTION, INTERACTION WITH CCNY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-164.
RX PubMed=19524571; DOI=10.1016/j.febslet.2009.06.010;
RA Jiang M., Gao Y., Yang T., Zhu X., Chen J.;
RT "Cyclin Y, a novel membrane-associated cyclin, interacts with PFTK1.";
RL FEBS Lett. 583:2171-2178(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-78 AND SER-134, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP IDENTIFICATION IN A COMPLEX WITH CAPRIN2; LRP6 AND CCNY.
RX PubMed=27821587; DOI=10.1074/jbc.m116.744607;
RA Wang X., Jia Y., Fei C., Song X., Li L.;
RT "Caprin-2 positively regulates CDK14/Cyclin Y-mediated LRP5/6 constitutive
RT phosphorylation.";
RL J. Biol. Chem. 291:26427-26434(2016).
RN [19]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-432 AND ARG-463.
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: Serine/threonine-protein kinase involved in the control of
CC the eukaryotic cell cycle, whose activity is controlled by an
CC associated cyclin. Acts as a cell-cycle regulator of Wnt signaling
CC pathway during G2/M phase by mediating the phosphorylation of LRP6 at
CC 'Ser-1490', leading to the activation of the Wnt signaling pathway.
CC Acts as a regulator of cell cycle progression and cell proliferation
CC via its interaction with CCDN3. Phosphorylates RB1 in vitro, however
CC the relevance of such result remains to be confirmed in vivo. May also
CC play a role in meiosis, neuron differentiation and may indirectly act
CC as a negative regulator of insulin-responsive glucose transport.
CC {ECO:0000269|PubMed:16461467, ECO:0000269|PubMed:17517622,
CC ECO:0000269|PubMed:19524571, ECO:0000269|PubMed:20059949}.
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 -!- ACTIVITY REGULATION: Serine/threonine-protein kinase activity is
CC promoted by associated cyclins CCDN3 and CCNY and repressed by CDKN1A.
CC -!- SUBUNIT: Found in a complex with LRP6, CCNY and CAPRIN2 during G2/M
CC stage; CAPRIN2 functions as a scaffold for the complex by binding to
CC CCNY via its N terminus and to CDK14 via its C terminus
CC (PubMed:27821587). Interacts with CCNY; CCNY mediates its recruitment
CC to the plasma membrane and promotes phosphorylation of LRP6
CC (PubMed:20059949, PubMed:19524571). Interacts with CCDN3 and CDKN1A
CC (PubMed:17517622). Interacts with SEPT8 (PubMed:12098780). Interacts
CC with 14-3-3 proteina YWHAB, YWHAE, YWHAH and YWHAQ (PubMed:16775625).
CC {ECO:0000269|PubMed:12098780, ECO:0000269|PubMed:16775625,
CC ECO:0000269|PubMed:17517622, ECO:0000269|PubMed:19524571,
CC ECO:0000269|PubMed:20059949, ECO:0000269|PubMed:27821587}.
CC -!- INTERACTION:
CC O94921; P30281: CCND3; NbExp=5; IntAct=EBI-1043945, EBI-375013;
CC O94921; Q8ND76: CCNY; NbExp=7; IntAct=EBI-1043945, EBI-1049189;
CC O94921; P38936: CDKN1A; NbExp=8; IntAct=EBI-1043945, EBI-375077;
CC O94921; P08238: HSP90AB1; NbExp=2; IntAct=EBI-1043945, EBI-352572;
CC O94921; P31946: YWHAB; NbExp=5; IntAct=EBI-1043945, EBI-359815;
CC O94921; P62258: YWHAE; NbExp=3; IntAct=EBI-1043945, EBI-356498;
CC O94921; Q04917: YWHAH; NbExp=4; IntAct=EBI-1043945, EBI-306940;
CC O94921; P27348: YWHAQ; NbExp=3; IntAct=EBI-1043945, EBI-359854;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Cytoplasm. Nucleus. Note=Recruited to the cell membrane by CCNY.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O94921-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94921-2; Sequence=VSP_004803;
CC Name=3;
CC IsoId=O94921-3; Sequence=VSP_038762;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, pancreas, kidney, heart,
CC testis and ovary. Also detected at lower levels in other tissues except
CC in spleen and thymus where expression is barely detected.
CC {ECO:0000269|PubMed:11313143}.
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=BAA74857.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF119833; AAG43234.1; -; mRNA.
DR EMBL; AB020641; BAA74857.2; ALT_INIT; mRNA.
DR EMBL; AK289782; BAF82471.1; -; mRNA.
DR EMBL; AK295086; BAG58127.1; -; mRNA.
DR EMBL; AK297974; BAG60284.1; -; mRNA.
DR EMBL; AK316026; BAH14397.1; -; mRNA.
DR EMBL; AC000057; AAS07411.1; -; Genomic_DNA.
DR EMBL; AC000059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002065; AAM48566.1; -; Genomic_DNA.
DR EMBL; AC002456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002458; AAS07412.1; -; Genomic_DNA.
DR EMBL; AC006036; AAF19245.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24162.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76873.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76874.1; -; Genomic_DNA.
DR EMBL; BC136476; AAI36477.1; -; mRNA.
DR EMBL; BC136477; AAI36478.1; -; mRNA.
DR EMBL; BC152388; AAI52389.1; -; mRNA.
DR EMBL; BC152436; AAI52437.1; -; mRNA.
DR EMBL; BC167152; AAI67152.1; -; mRNA.
DR EMBL; BC167156; AAI67156.1; -; mRNA.
DR CCDS; CCDS5619.1; -. [O94921-2]
DR CCDS; CCDS75626.1; -. [O94921-1]
DR CCDS; CCDS75627.1; -. [O94921-3]
DR RefSeq; NP_001274064.1; NM_001287135.1. [O94921-1]
DR RefSeq; NP_001274065.1; NM_001287136.1. [O94921-3]
DR RefSeq; NP_001274066.1; NM_001287137.1.
DR RefSeq; NP_036527.1; NM_012395.3. [O94921-2]
DR RefSeq; XP_005250495.1; XM_005250438.3.
DR RefSeq; XP_005250496.1; XM_005250439.2.
DR RefSeq; XP_011514608.1; XM_011516306.2.
DR RefSeq; XP_016867809.1; XM_017012320.1.
DR RefSeq; XP_016867810.1; XM_017012321.1.
DR RefSeq; XP_016867811.1; XM_017012322.1.
DR AlphaFoldDB; O94921; -.
DR SMR; O94921; -.
DR BioGRID; 111239; 36.
DR ComplexPortal; CPX-364; Cyclin Y-CDK14 complex.
DR DIP; DIP-39618N; -.
DR IntAct; O94921; 23.
DR MINT; O94921; -.
DR STRING; 9606.ENSP00000369390; -.
DR BindingDB; O94921; -.
DR ChEMBL; CHEMBL6162; -.
DR DrugCentral; O94921; -.
DR iPTMnet; O94921; -.
DR PhosphoSitePlus; O94921; -.
DR BioMuta; CDK14; -.
DR EPD; O94921; -.
DR jPOST; O94921; -.
DR MassIVE; O94921; -.
DR MaxQB; O94921; -.
DR PaxDb; O94921; -.
DR PeptideAtlas; O94921; -.
DR PRIDE; O94921; -.
DR ProteomicsDB; 50556; -. [O94921-1]
DR ProteomicsDB; 50557; -. [O94921-2]
DR ProteomicsDB; 50558; -. [O94921-3]
DR Antibodypedia; 15462; 238 antibodies from 28 providers.
DR DNASU; 5218; -.
DR Ensembl; ENST00000265741.7; ENSP00000265741.3; ENSG00000058091.17. [O94921-2]
DR Ensembl; ENST00000380050.8; ENSP00000369390.3; ENSG00000058091.17. [O94921-1]
DR Ensembl; ENST00000406263.5; ENSP00000385034.1; ENSG00000058091.17. [O94921-3]
DR GeneID; 5218; -.
DR KEGG; hsa:5218; -.
DR MANE-Select; ENST00000380050.8; ENSP00000369390.3; NM_001287135.2; NP_001274064.1.
DR UCSC; uc003uky.4; human. [O94921-1]
DR CTD; 5218; -.
DR DisGeNET; 5218; -.
DR GeneCards; CDK14; -.
DR HGNC; HGNC:8883; CDK14.
DR HPA; ENSG00000058091; Low tissue specificity.
DR MIM; 610679; gene.
DR neXtProt; NX_O94921; -.
DR OpenTargets; ENSG00000058091; -.
DR PharmGKB; PA33221; -.
DR VEuPathDB; HostDB:ENSG00000058091; -.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000157640; -.
DR InParanoid; O94921; -.
DR OMA; NSRHGCA; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; O94921; -.
DR TreeFam; TF106508; -.
DR PathwayCommons; O94921; -.
DR SignaLink; O94921; -.
DR SIGNOR; O94921; -.
DR BioGRID-ORCS; 5218; 8 hits in 1100 CRISPR screens.
DR ChiTaRS; CDK14; human.
DR GeneWiki; PFTK1; -.
DR GenomeRNAi; 5218; -.
DR Pharos; O94921; Tchem.
DR PRO; PR:O94921; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O94921; protein.
DR Bgee; ENSG00000058091; Expressed in postcentral gyrus and 191 other tissues.
DR ExpressionAtlas; O94921; baseline and differential.
DR Genevisible; O94921; HS.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000308; C:cytoplasmic cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell membrane; Cytoplasm; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Wnt signaling pathway.
FT CHAIN 1..469
FT /note="Cyclin-dependent kinase 14"
FT /id="PRO_0000086506"
FT DOMAIN 135..419
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 103..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 141..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10048485"
FT /id="VSP_038762"
FT VAR_SEQ 1..41
FT /note="MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKDDTTFDE -> MHGYFGC
FT NAAAEPGYSAFVGTPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10048485,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_004803"
FT VARIANT 432
FT /note="M -> I (in an ovarian mucinous carcinoma; somatic
FT mutation; dbSNP:rs773301216)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_046765"
FT VARIANT 463
FT /note="S -> R (in dbSNP:rs35643773)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_046766"
FT MUTAGEN 164
FT /note="K->R: Abolishes protein kinase activity."
FT /evidence="ECO:0000269|PubMed:17517622,
FT ECO:0000269|PubMed:19524571"
FT CONFLICT 8
FT /note="Q -> R (in Ref. 3; BAG60284)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="G -> W (in Ref. 1; AAG43234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 53057 MW; 32CF9B9B7BD9CE0E CRC64;
MCDLIEPQPA EKIGKMKKLR RTLSESFSRI ALKKDDTTFD EICVTKMSTR NCQGMDSVIK
PLDTIPEDKK VRVQRTQSTF DPFEKPANQV KRVHSENNAC INFKTSSTGK ESPKVRRHSS
PSSPTSPKFG KADSYEKLEK LGEGSYATVY KGKSKVNGKL VALKVIRLQE EEGTPFTAIR
EASLLKGLKH ANIVLLHDII HTKETLTLVF EYVHTDLCQY MDKHPGGLHP DNVKLFLFQL
LRGLSYIHQR YILHRDLKPQ NLLISDTGEL KLADFGLARA KSVPSHTYSN EVVTLWYRPP
DVLLGSTEYS TCLDMWGVGC IFVEMIQGVA AFPGMKDIQD QLERIFLVLG TPNEDTWPGV
HSLPHFKPER FTLYSSKNLR QAWNKLSYVN HAEDLASKLL QCSPKNRLSA QAALSHEYFS
DLPPRLWELT DMSSIFTVPN VRLQPEAGES MRAFGKNNSY GKSLSNSKH
