ID CDK1_HUMAN Reviewed; 297 AA. AC P06493; A8K7C4; C9J497; O60764; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 31-MAY-2011, sequence version 3. DT 27-MAR-2024, entry version 271. DE RecName: Full=Cyclin-dependent kinase 1; DE Short=CDK1; DE EC=2.7.11.22 {ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:30704899}; DE EC=2.7.11.23 {ECO:0000250|UniProtKB:P11440}; DE AltName: Full=Cell division control protein 2 homolog; DE AltName: Full=Cell division protein kinase 1; DE AltName: Full=p34 protein kinase; GN Name=CDK1; Synonyms=CDC2, CDC28A, CDKN1, P34CDC2; 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). RX PubMed=3553962; DOI=10.1038/327031a0; RA Lee M.G., Nurse P.; RT "Complementation used to clone a human homologue of the fission yeast cell RT cycle control gene cdc2."; RL Nature 327:31-35(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. RC TISSUE=Mammary cancer; RX PubMed=9515786; RA Ohta T., Okamoto K., Isohashi F., Shibata K., Fukuda M., Yamaguchi S., RA Xiong Y.; RT "T-loop deletion of CDC2 from breast cancer tissues eliminates binding to RT cyclin B1 and cyclin-dependent kinase inhibitor p21."; RL Cancer Res. 58:1095-1098(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [7] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [9] RP ASSOCIATION WITH P13. RX PubMed=3289755; DOI=10.1016/0092-8674(88)90175-4; RA Draetta G., Beach D.; RT "Activation of cdc2 protein kinase during mitosis in human cells: cell RT cycle-dependent phosphorylation and subunit rearrangement."; RL Cell 54:17-26(1988). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION IN THE MPF COMPLEX. RX PubMed=2344612; DOI=10.1016/0092-8674(90)90470-y; RA Heald R., McKeon F.; RT "Mutations of phosphorylation sites in lamin A that prevent nuclear lamina RT disassembly in mitosis."; RL Cell 61:579-589(1990). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION IN THE MPF COMPLEX. RX PubMed=2188730; DOI=10.1016/0092-8674(90)90469-u; RA Ward G.E., Kirschner M.W.; RT "Identification of cell cycle-regulated phosphorylation sites on nuclear RT lamin C."; RL Cell 61:561-577(1990). RN [12] RP ACTIVITY REGULATION, AND PHOSPHORYLATION AT THR-14 AND TYR-15 BY PKMYT1. RX PubMed=7569953; DOI=10.1126/science.270.5233.86; RA Mueller P.R., Coleman T.R., Kumagai A., Dunphy W.G.; RT "Myt1: a membrane-associated inhibitory kinase that phosphorylates Cdc2 on RT both threonine-14 and tyrosine-15."; RL Science 270:86-90(1995). RN [13] RP INTERACTION WITH FANCC. RX PubMed=9242535; RA Kupfer G.M., Yamashita T., Naf D., Suliman A., Asano S., D'Andrea A.D.; RT "The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase, RT cdc2."; RL Blood 90:1047-1054(1997). RN [14] RP ACTIVITY REGULATION BY ROSCOVITINE AND OLOMOUCINE. RX PubMed=9030781; DOI=10.1111/j.1432-1033.1997.t01-2-00527.x; RA Meijer L., Borgne A., Mulner O., Chong J.P.J., Blow J.J., Inagaki N., RA Inagaki M., Delcros J.-G., Moulinoux J.-P.; RT "Biochemical and cellular effects of roscovitine, a potent and selective RT inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5."; RL Eur. J. Biochem. 243:527-536(1997). RN [15] RP INTERACTION WITH RALBP1. RX PubMed=12775724; DOI=10.1074/jbc.m302191200; RA Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.; RT "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to RT phosphorylate epsin during the switch off of endocytosis in mitosis."; RL J. Biol. Chem. 278:30597-30604(2003). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [17] RP INTERACTION WITH DLGAP5. RX PubMed=15145941; DOI=10.1074/jbc.m404950200; RA Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.; RT "Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated RT hepatoma up-regulated protein (HURP) proteolysis by a proline-rich RT region."; RL J. Biol. Chem. 279:32592-32602(2004). RN [18] RP FUNCTION AS RUNX2 KINASE. RX PubMed=16407259; DOI=10.1074/jbc.m508162200; RA Qiao M., Shapiro P., Fosbrink M., Rus H., Kumar R., Passaniti A.; RT "Cell cycle-dependent phosphorylation of the RUNX2 transcription factor by RT cdc2 regulates endothelial cell proliferation."; RL J. Biol. Chem. 281:7118-7128(2006). RN [19] RP FUNCTION AS BETA-TUBULINS KINASE. RX PubMed=16371510; DOI=10.1091/mbc.e05-07-0621; RA Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I., Juillan-Binard C., RA Lantez V., Job D.; RT "Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin- RT dependent kinase Cdk1."; RL Mol. Biol. Cell 17:1041-1050(2006). RN [20] RP INDUCTION BY CKS1B. RX PubMed=18056467; DOI=10.1158/0008-5472.can-06-4173; RA Westbrook L., Manuvakhova M., Kern F.G., Estes N.R. II, Ramanathan H.N., RA Thottassery J.V.; RT "Cks1 regulates cdk1 expression: a novel role during mitotic entry in RT breast cancer cells."; RL Cancer Res. 67:11393-11401(2007). RN [21] RP FUNCTION AS RB1 KINASE, ACTIVITY REGULATION BY TGFB1, AND REPRESSION BY RP TGFB1. RX PubMed=17459720; DOI=10.1016/j.cyto.2007.03.009; RA Hu X., Cui D., Moscinski L.C., Zhang X., Maccachero V., Zuckerman K.S.; RT "TGFbeta regulates the expression and activities of G2 checkpoint kinases RT in human myeloid leukemia cells."; RL Cytokine 37:155-162(2007). RN [22] RP FUNCTION AS SIRT2 KINASE, AND SUBCELLULAR LOCATION. RX PubMed=16933150; DOI=10.1007/s11064-006-9127-6; RA Southwood C.M., Peppi M., Dryden S., Tainsky M.A., Gow A.; RT "Microtubule deacetylases, SirT2 and HDAC6, in the nervous system."; RL Neurochem. Res. 32:187-195(2007). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [24] RP FUNCTION DURING THE M PHASE, AND MUTAGENESIS OF 14-THR-TYR-15. RX PubMed=18480403; DOI=10.1091/mbc.e08-02-0172; RA Pomerening J.R., Ubersax J.A., Ferrell J.E. Jr.; RT "Rapid cycling and precocious termination of G1 phase in cells expressing RT CDK1AF."; RL Mol. Biol. Cell 19:3426-3441(2008). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19; SER-39; TYR-77 AND RP THR-222, AND IDENTIFICATION BY 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 [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, AND RP IDENTIFICATION BY 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 [27] RP FUNCTION AS FOXO1 KINASE. RX PubMed=18356527; DOI=10.1126/science.1152337; RA Yuan Z., Becker E.B.E., Merlo P., Yamada T., DiBacco S., Konishi Y., RA Schaefer E.M., Bonni A.; RT "Activation of FOXO1 by Cdk1 in cycling cells and postmitotic neurons."; RL Science 319:1665-1668(2008). RN [28] RP FUNCTION AS NEDD1 KINASE. RX PubMed=19509060; DOI=10.1242/jcs.042747; RA Zhang X., Chen Q., Feng J., Hou J., Yang F., Liu J., Jiang Q., Zhang C.; RT "Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for RT targeting of the gammaTuRC to the centrosome."; RL J. Cell Sci. 122:2240-2251(2009). RN [29] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT TYR-19; SER-39; SER-178; THR-222 AND SER-248, AND RP IDENTIFICATION BY 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 [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15 AND THR-161, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [31] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [32] RP FUNCTION AS CC2D1A KINASE. RX PubMed=20171170; DOI=10.1016/j.bbrc.2010.02.103; RA Nakamura A., Naito M., Arai H., Fujita N.; RT "Mitotic phosphorylation of Aki1 at Ser208 by cyclin B1-Cdk1 complex."; RL Biochem. Biophys. Res. Commun. 393:872-876(2010). RN [33] RP FUNCTION IN G2 ARREST UPON DNA DAMAGE, PHOSPHORYLATION AT TYR-4 BY RP PKR/EIF2AK2, POLYUBIQUITINATION, AND MUTAGENESIS OF TYR-4. RX PubMed=20395957; DOI=10.1038/embor.2010.45; RA Yoon C.-H., Miah M.A., Kim K.P., Bae Y.-S.; RT "New Cdc2 Tyr 4 phosphorylation by dsRNA-activated protein kinase triggers RT Cdc2 polyubiquitination and G2 arrest under genotoxic stresses."; RL EMBO Rep. 11:393-399(2010). RN [34] RP PHOSPHORYLATION AT TYR-15. RX PubMed=19917613; DOI=10.1074/jbc.m109.055392; RA LaGory E.L., Sitailo L.A., Denning M.F.; RT "The protein kinase Cdelta catalytic fragment is critical for maintenance RT of the G2/M DNA damage checkpoint."; RL J. Biol. Chem. 285:1879-1887(2010). RN [35] RP FUNCTION IN G2-M TRANSITION, ACTIVITY REGULATION, DEPHOSPHORYLATION AT RP THR-14 AND TYR-15 BY CDC25, PHOSPHORYLATION AT THR-161 BY CDK7/CAK, AND RP INTERACTION WITH B-CYCLIN. RX PubMed=20360007; DOI=10.1074/jbc.m109.096552; RA Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.; RT "Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B at RT the G2/M transition."; RL J. Biol. Chem. 285:16978-16990(2010). RN [36] RP FUNCTION AS BCL-XL/BCL2L1 KINASE, AND SUBCELLULAR LOCATION. RX PubMed=19917720; DOI=10.1128/mcb.00882-09; RA Terrano D.T., Upreti M., Chambers T.C.; RT "Cyclin-dependent kinase 1-mediated Bcl-xL/Bcl-2 phosphorylation acts as a RT functional link coupling mitotic arrest and apoptosis."; RL Mol. Cell. Biol. 30:640-656(2010). RN [37] RP FUNCTION AS CASP8 KINASE. RX PubMed=20937773; DOI=10.1128/mcb.00731-10; RA Matthess Y., Raab M., Sanhaji M., Lavrik I.N., Strebhardt K.; RT "Cdk1/cyclin B1 controls Fas-mediated apoptosis by regulating caspase-8 RT activity."; RL Mol. Cell. Biol. 30:5726-5740(2010). RN [38] RP FUNCTION AS EZH2 KINASE. RX PubMed=20935635; DOI=10.1038/ncb2116; RA Chen S., Bohrer L.R., Rai A.N., Pan Y., Gan L., Zhou X., Bagchi A., RA Simon J.A., Huang H.; RT "Cyclin-dependent kinases regulate epigenetic gene silencing through RT phosphorylation of EZH2."; RL Nat. Cell Biol. 12:1108-1114(2010). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [40] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [41] RP INTERACTION WITH CEP63, AND SUBCELLULAR LOCATION. RX PubMed=21406398; DOI=10.1158/0008-5472.can-10-2684; RA Loffler H., Fechter A., Matuszewska M., Saffrich R., Mistrik M., RA Marhold J., Hornung C., Westermann F., Bartek J., Kramer A.; RT "Cep63 recruits Cdk1 to the centrosome: implications for regulation of RT mitotic entry, centrosome amplification, and genome maintenance."; RL Cancer Res. 71:2129-2139(2011). RN [42] RP FUNCTION AS CHAMP1 KINASE. RX PubMed=21063390; DOI=10.1038/emboj.2010.276; RA Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., RA Mizuno K., Yasui A., Hirota T., Tanaka K.; RT "CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule RT attachment."; RL EMBO J. 30:130-144(2011). RN [43] RP REVIEW ON SUBSTRATES, AND GENE FAMILY. RX PubMed=16236519; DOI=10.1016/j.tibs.2005.09.005; RA Malumbres M., Barbacid M.; RT "Mammalian cyclin-dependent kinases."; RL Trends Biochem. Sci. 30:630-641(2005). RN [44] RP REVIEW ON SUBCELLULAR TRANSLOCATION. RX PubMed=19364923; DOI=10.1083/jcb.200812045; RA Lindqvist A., Rodriguez-Bravo V., Medema R.H.; RT "The decision to enter mitosis: feedback and redundancy in the mitotic RT entry network."; RL J. Cell Biol. 185:193-202(2009). RN [45] RP REVIEW ON CELL CYCLE CONTROL AND INHIBITORS, AND GENE FAMILY. RX PubMed=19238148; DOI=10.1038/nrc2602; RA Malumbres M., Barbacid M.; RT "Cell cycle, CDKs and cancer: a changing paradigm."; RL Nat. Rev. Cancer 9:153-166(2009). RN [46] RP REVIEW ON CELL CYCLE CONTROL. RX PubMed=21535261; DOI=10.1111/j.1365-2184.2011.00753.x; RA Hu X., Moscinski L.C.; RT "Cdc2: a monopotent or pluripotent CDK?"; RL Cell Prolif. 44:205-211(2011). RN [47] RP REVIEW ON CELL CYCLE CONTROL AND INHIBITORS. RX PubMed=21517772; DOI=10.2174/092986711795590110; RA Wang Q., Su L., Liu N., Zhang L., Xu W., Fang H.; RT "Cyclin dependent kinase 1 inhibitors: a review of recent progress."; RL Curr. Med. Chem. 18:2025-2043(2011). RN [48] RP REVIEW ON CELL CYCLE CONTROL. RX PubMed=21655336; DOI=10.3410/b3-10; RA Medema R.H., Macurek L.; RT "Checkpoint recovery in cells: how a molecular understanding can help in RT the fight against cancer."; RL F1000 Biol. Rep. 3:10-10(2011). RN [49] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=21516087; DOI=10.1038/nm.2341; RA Lupberger J., Zeisel M.B., Xiao F., Thumann C., Fofana I., Zona L., RA Davis C., Mee C.J., Turek M., Gorke S., Royer C., Fischer B., Zahid M.N., RA Lavillette D., Fresquet J., Cosset F.L., Rothenberg S.M., Pietschmann T., RA Patel A.H., Pessaux P., Doffoel M., Raffelsberger W., Poch O., RA McKeating J.A., Brino L., Baumert T.F.; RT "EGFR and EphA2 are host factors for hepatitis C virus entry and possible RT targets for antiviral therapy."; RL Nat. Med. 17:589-595(2011). RN [50] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [51] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [52] RP FUNCTION. RX PubMed=23602554; DOI=10.1016/j.celrep.2013.03.017; RA Cribier A., Descours B., Valadao A.L., Laguette N., Benkirane M.; RT "Phosphorylation of SAMHD1 by cyclin A2/CDK1 regulates its restriction RT activity toward HIV-1."; RL Cell Rep. 3:1036-1043(2013). RN [53] RP FUNCTION. RX PubMed=23601106; DOI=10.1016/j.chom.2013.03.005; RA White T.E., Brandariz-Nunez A., Valle-Casuso J.C., Amie S., Nguyen L.A., RA Kim B., Tuzova M., Diaz-Griffero F.; RT "The retroviral restriction ability of SAMHD1, but not its deoxynucleotide RT triphosphohydrolase activity, is regulated by phosphorylation."; RL Cell Host Microbe 13:441-451(2013). RN [54] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23355470; DOI=10.1074/jbc.m112.441048; RA Schofield A.V., Gamell C., Suryadinata R., Sarcevic B., Bernard O.; RT "Tubulin polymerization promoting protein 1 (Tppp1) phosphorylation by Rho- RT associated coiled-coil kinase (rock) and cyclin-dependent kinase 1 (Cdk1) RT inhibits microtubule dynamics to increase cell proliferation."; RL J. Biol. Chem. 288:7907-7917(2013). RN [55] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; THR-141 AND THR-161, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; 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 [56] RP FUNCTION. RX PubMed=26549230; DOI=10.1016/j.bbrc.2015.11.004; RA Mori Y., Inoue Y., Taniyama Y., Tanaka S., Terada Y.; RT "Phosphorylation of the centrosomal protein, Cep169, by Cdk1 promotes its RT dissociation from centrosomes in mitosis."; RL Biochem. Biophys. Res. Commun. 468:642-646(2015). RN [57] RP FUNCTION, AND INTERACTION WITH CENPA. RX PubMed=25556658; DOI=10.1016/j.devcel.2014.11.030; RA Yu Z., Zhou X., Wang W., Deng W., Fang J., Hu H., Wang Z., Li S., Cui L., RA Shen J., Zhai L., Peng S., Wong J., Dong S., Yuan Z., Ou G., Zhang X., RA Xu P., Lou J., Yang N., Chen P., Xu R.M., Li G.; RT "Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle- RT dependent deposition at centromeres."; RL Dev. Cell 32:68-81(2015). RN [58] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [59] RP FUNCTION, AND INTERACTION WITH NR1D1. RX PubMed=27238018; DOI=10.1016/j.cell.2016.05.012; RA Zhao X., Hirota T., Han X., Cho H., Chong L.W., Lamia K., Liu S., RA Atkins A.R., Banayo E., Liddle C., Yu R.T., Yates J.R. III, Kay S.A., RA Downes M., Evans R.M.; RT "Circadian amplitude regulation via FBXW7-targeted REV-ERBalpha RT degradation."; RL Cell 165:1644-1657(2016). RN [60] RP FUNCTION. RX PubMed=26829474; DOI=10.1038/nchembio.2017; RA Mo F., Zhuang X., Liu X., Yao P.Y., Qin B., Su Z., Zang J., Wang Z., RA Zhang J., Dou Z., Tian C., Teng M., Niu L., Hill D.L., Fang G., Ding X., RA Fu C., Yao X.; RT "Acetylation of Aurora B by TIP60 ensures accurate chromosomal RT segregation."; RL Nat. Chem. Biol. 12:226-232(2016). RN [61] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-20 AND LYS-139, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [62] RP PHOSPHORYLATION AT TYR-15. RX PubMed=29606300; DOI=10.1016/j.ajhg.2018.02.015; RA Sang Q., Li B., Kuang Y., Wang X., Zhang Z., Chen B., Wu L., Lyu Q., Fu Y., RA Yan Z., Mao X., Xu Y., Mu J., Li Q., Jin L., He L., Wang L.; RT "Homozygous Mutations in WEE2 Cause Fertilization Failure and Female RT Infertility."; RL Am. J. Hum. Genet. 102:649-657(2018). RN [63] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=30139873; DOI=10.1126/science.aap9346; RA Saldivar J.C., Hamperl S., Bocek M.J., Chung M., Bass T.E., RA Cisneros-Soberanis F., Samejima K., Xie L., Paulson J.R., Earnshaw W.C., RA Cortez D., Meyer T., Cimprich K.A.; RT "An intrinsic S/G2 checkpoint enforced by ATR."; RL Science 361:806-810(2018). RN [64] RP FUNCTION AS EML3 KINASE. RX PubMed=30723163; DOI=10.1074/jbc.ra118.007164; RA Luo J., Yang B., Xin G., Sun M., Zhang B., Guo X., Jiang Q., Zhang C.; RT "The microtubule-associated protein EML3 regulates mitotic spindle assembly RT by recruiting the Augmin complex to spindle microtubules."; RL J. Biol. Chem. 294:5643-5656(2019). RN [65] RP FUNCTION. RX PubMed=30704899; DOI=10.1016/j.molcel.2018.12.017; RA Cheng X., Ma X., Zhu Q., Song D., Ding X., Li L., Jiang X., Wang X., RA Tian R., Su H., Shen Z., Chen S., Liu T., Gong W., Liu W., Sun Q.; RT "Pacer is a mediator of mTORC1 and GSK3-TIP60 signaling in regulation of RT autophagosome maturation and lipid metabolism."; RL Mol. Cell 73:1-15(2019). RN [66] RP FUNCTION AS CGAS KINASE. RX PubMed=32351706; DOI=10.1038/s41421-020-0162-2; RA Zhong L., Hu M.M., Bian L.J., Liu Y., Chen Q., Shu H.B.; RT "Phosphorylation of cGAS by CDK1 impairs self-DNA sensing in mitosis."; RL Cell Discov. 6:26-26(2020). RN [67] RP INTERACTION WITH SFTSV VIRUS NSS (MICROBIAL INFECTION). RX PubMed=31852787; DOI=10.1128/jvi.01575-19; RA Liu S., Liu H., Kang J., Xu L., Zhang K., Li X., Hou W., Wang Z., Wang T.; RT "The Severe Fever with Thrombocytopenia Syndrome Virus NSs Protein RT Interacts with CDK1 To Induce G2 Cell Cycle Arrest and Positively Regulate RT Viral Replication."; RL J. Virol. 94:0-0(2020). RN [68] RP FUNCTION. RX PubMed=34741373; DOI=10.1111/cas.15188; RA Zhang E., Chen S., Tang H., Fei C., Yuan Z., Mu X., Qin Y., Liu H., Fan Y., RA Tan M., Wang X.; RT "CDK1/FBXW7 facilitates degradation and ubiquitination of MLST8 to inhibit RT progression of renal cell carcinoma."; RL Cancer Sci. 113:91-108(2022). RN [69] RP FUNCTION. RX PubMed=37788673; DOI=10.1016/j.molcel.2023.09.003; RA Joo Y.K., Black E.M., Trier I., Haakma W., Zou L., Kabeche L.; RT "ATR promotes clearance of damaged DNA and damaged cells by rupturing RT micronuclei."; RL Mol. Cell 83:3642-3658(2023). CC -!- FUNCTION: Plays a key role in the control of the eukaryotic cell cycle CC by modulating the centrosome cycle as well as mitotic onset; promotes CC G2-M transition via association with multiple interphase cyclins CC (PubMed:2344612, PubMed:2188730, PubMed:16407259, PubMed:17459720, CC PubMed:16933150, PubMed:18356527, PubMed:19509060, PubMed:20171170, CC PubMed:19917720, PubMed:20937773, PubMed:20935635, PubMed:21063390, CC PubMed:23355470, PubMed:23601106, PubMed:23602554, PubMed:25556658, CC PubMed:26829474, PubMed:30139873, PubMed:30704899). Phosphorylates CC PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CC CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CENPA, CSNK2 proteins/CKII, CC FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, CC EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, CC UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, KAT5, CC LMNA, LMNB, LBR, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MLST8, CC MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, CC NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, CC NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, TPPP, UL40/R2, RAB4A, RAP1GAP, CC RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, CC TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, CC RUNX1/AML1, SAMHD1, SIRT2, CGAS and RUNX2 (PubMed:2344612, CC PubMed:2188730, PubMed:16407259, PubMed:17459720, PubMed:16933150, CC PubMed:18356527, PubMed:19509060, PubMed:20171170, PubMed:19917720, CC PubMed:20937773, PubMed:20935635, PubMed:21063390, PubMed:23355470, CC PubMed:23601106, PubMed:23602554, PubMed:25556658, PubMed:32351706, CC PubMed:26829474, PubMed:30704899, PubMed:34741373). CDK1/CDC2-cyclin-B CC controls pronuclear union in interphase fertilized eggs CC (PubMed:18480403, PubMed:20360007). Essential for early stages of CC embryonic development (PubMed:18480403, PubMed:20360007). During G2 and CC early mitosis, CDC25A/B/C-mediated dephosphorylation activates CC CDK1/cyclin complexes which phosphorylate several substrates that CC trigger at least centrosome separation, Golgi dynamics, nuclear CC envelope breakdown and chromosome condensation (PubMed:2344612, CC PubMed:2188730, PubMed:18480403, PubMed:20360007, PubMed:30139873). CC Once chromosomes are condensed and aligned at the metaphase plate, CDK1 CC activity is switched off by WEE1- and PKMYT1-mediated phosphorylation CC to allow sister chromatid separation, chromosome decondensation, CC reformation of the nuclear envelope and cytokinesis (PubMed:18480403, CC PubMed:20360007). Phosphorylates KRT5 during prometaphase and metaphase CC (By similarity). Inactivated by PKR/EIF2AK2- and WEE1-mediated CC phosphorylation upon DNA damage to stop cell cycle and genome CC replication at the G2 checkpoint thus facilitating DNA repair CC (PubMed:20360007). Reactivated after successful DNA repair through CC WIP1-dependent signaling leading to CDC25A/B/C-mediated CC dephosphorylation and restoring cell cycle progression CC (PubMed:20395957). Catalyzes lamin (LMNA, LMNB1 and LMNB2) CC phosphorylation at the onset of mitosis, promoting nuclear envelope CC breakdown (PubMed:2344612, PubMed:2188730, PubMed:37788673). In CC proliferating cells, CDK1-mediated FOXO1 phosphorylation at the G2-M CC phase represses FOXO1 interaction with 14-3-3 proteins and thereby CC promotes FOXO1 nuclear accumulation and transcription factor activity, CC leading to cell death of postmitotic neurons (PubMed:18356527). The CC phosphorylation of beta-tubulins regulates microtubule dynamics during CC mitosis (PubMed:16371510). NEDD1 phosphorylation promotes PLK1-mediated CC NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin CC ring complex (gTuRC) to the centrosome, an important step for spindle CC formation (PubMed:19509060). In addition, CC2D1A phosphorylation CC regulates CC2D1A spindle pole localization and association with CC SCC1/RAD21 and centriole cohesion during mitosis (PubMed:20171170). The CC phosphorylation of Bcl-xL/BCL2L1 after prolongated G2 arrest upon DNA CC damage triggers apoptosis (PubMed:19917720). In contrast, CASP8 CC phosphorylation during mitosis prevents its activation by proteolysis CC and subsequent apoptosis (PubMed:20937773). This phosphorylation occurs CC in cancer cell lines, as well as in primary breast tissues and CC lymphocytes (PubMed:20937773). EZH2 phosphorylation promotes H3K27me3 CC maintenance and epigenetic gene silencing (PubMed:20935635). CALD1 CC phosphorylation promotes Schwann cell migration during peripheral nerve CC regeneration (By similarity). CDK1-cyclin-B complex phosphorylates CC NCKAP5L and mediates its dissociation from centrosomes during mitosis CC (PubMed:26549230). Regulates the amplitude of the cyclic expression of CC the core clock gene BMAL1 by phosphorylating its transcriptional CC repressor NR1D1, and this phosphorylation is necessary for SCF(FBXW7)- CC mediated ubiquitination and proteasomal degradation of NR1D1 CC (PubMed:27238018). Phosphorylates EML3 at 'Thr-881' which is essential CC for its interaction with HAUS augmin-like complex and TUBG1 CC (PubMed:30723163). Phosphorylates CGAS during mitosis, leading to its CC inhibition, thereby preventing CGAS activation by self DNA during CC mitosis (PubMed:32351706). {ECO:0000250|UniProtKB:P11440, CC ECO:0000250|UniProtKB:P39951, ECO:0000269|PubMed:16371510, CC ECO:0000269|PubMed:16407259, ECO:0000269|PubMed:16933150, CC ECO:0000269|PubMed:17459720, ECO:0000269|PubMed:18356527, CC ECO:0000269|PubMed:18480403, ECO:0000269|PubMed:19509060, CC ECO:0000269|PubMed:19917720, ECO:0000269|PubMed:20171170, CC ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:20395957, CC ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:20937773, CC ECO:0000269|PubMed:21063390, ECO:0000269|PubMed:2188730, CC ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:2344612, CC ECO:0000269|PubMed:23601106, ECO:0000269|PubMed:23602554, CC ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:26549230, CC ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:27238018, CC ECO:0000269|PubMed:30139873, ECO:0000269|PubMed:30704899, CC ECO:0000269|PubMed:30723163, ECO:0000269|PubMed:32351706, CC ECO:0000269|PubMed:34741373, ECO:0000269|PubMed:37788673}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C CC virus (HCV) in hepatocytes and facilitates its cell entry. CC {ECO:0000269|PubMed:21516087}. 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:2188730, ECO:0000269|PubMed:23355470, CC ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:26829474, CC ECO:0000269|PubMed:30704899}; 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:23355470, CC ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:30704899}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho- CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA- CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, CC ChEBI:CHEBI:456216; EC=2.7.11.23; CC Evidence={ECO:0000250|UniProtKB:P11440}; CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates CC the enzyme, while phosphorylation at Thr-161 activates it CC (PubMed:7569953, PubMed:20360007). Activated through a multistep CC process; binding to cyclin-B is required for relocation of cyclin- CC kinase complexes to the nucleus, activated by CAK/CDK7-mediated CC phosphorylation on Thr-161, and CDC25-mediated dephosphorylation of CC inhibitory phosphorylation on Thr-14 and Tyr-15 (PubMed:7569953, CC PubMed:20360007). Activity is restricted during S-phase in an ATR- CC dependent manner to prevent premature entry into G2 (PubMed:30139873). CC Repressed by the CDK inhibitors CDKN1A/p21 and CDKN1B/p27 during the G1 CC phase and by CDKN1A/p21 at the G1-S checkpoint upon DNA damage. CC Transient activation by rapid and transient dephosphorylation at Tyr-15 CC triggered by TGFB1 (PubMed:17459720). Inhibited by flavopiridol and CC derivatives, pyrimidine derivatives, pyridine derivatives, purine CC derivatives, staurosporine, paullones, oxoindoles, indazole analogs, CC indolin-2-ones, pyrazolo[3,4-b]pyridines, imidazo[1,2-a]pyridine CC (AZ703), thiazolinone analogs(RO-3306), thiazol urea, macrocyclic CC quinoxalin-2-one, pyrrolo[2,3-a]carbazole, pyrazolo[1,5-a]-1,3,5- CC triazine, pyrazolo[1,5-a]pyrimidine (Dinaciclib, SCH 727965), 2-(1- CC ethyl-2-hydroxyethylamino)-6-benzylamino-9-isopropylpurine CC (roscovitine), olomoucine, AG-024322, AT-7519, P276-00, R547/Ro-4584820 CC and SNS-032/BMS-387032 (PubMed:9030781). {ECO:0000269|PubMed:17459720, CC ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:30139873, CC ECO:0000269|PubMed:7569953, ECO:0000269|PubMed:9030781}. CC -!- SUBUNIT: Forms a stable but non-covalent complex with a regulatory CC subunit and with a cyclin (PubMed:20360007). The cyclin subunit imparts CC substrate specificity to the complex (PubMed:20360007). Interacts with CC cyclins-B (CCNB1, CCNB2 and CCNB3) to form a serine/threonine kinase CC holoenzyme complex also known as maturation promoting factor (MPF) CC (PubMed:2344612, PubMed:2188730, PubMed:20360007). Promotes G2-M CC transition when in complex with a cyclin-B (PubMed:20360007). Can also CC form CDK1-cylin-D and CDK1-cyclin-E complexes that phosphorylate RB1 in CC vitro (PubMed:17459720). Associates with cyclins-A and B1 during S- CC phase in regenerating hepatocytes (PubMed:20360007). Interacts with CC DLGAP5 (PubMed:15145941). Binds to the CDK inhibitors CDKN1A/p21 and CC CDKN1B/p27. Interacts with catalytically active CCNB1 and RALBP1 during CC mitosis to form an endocytotic complex during interphase CC (PubMed:12775724). Interacts with FANCC (PubMed:9242535). Interacts CC with CEP63; this interaction recruits CDK1 to centrosomes CC (PubMed:21406398). Interacts with CENPA (PubMed:25556658). Interacts CC with NR1D1 (PubMed:27238018). Interacts with proteasome subunit PSMA8; CC to participate in meiosis progression during spermatogenesis (By CC similarity). {ECO:0000250|UniProtKB:P11440, CC ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:15145941, CC ECO:0000269|PubMed:17459720, ECO:0000269|PubMed:20360007, CC ECO:0000269|PubMed:21406398, ECO:0000269|PubMed:2188730, CC ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:25556658, CC ECO:0000269|PubMed:27238018, ECO:0000269|PubMed:9242535}. CC -!- SUBUNIT: [Isoform 2]: Unable to complex with cyclin-B1 and also fails CC to bind to CDKN1A/p21. {ECO:0000269|PubMed:9515786}. CC -!- SUBUNIT: (Microbial infection) Interacts with severe fever with CC thrombocytopenia syndrome virus (SFTSV) NSs; this interaction is CC inclusion body dependent, it inhibits the formation and nuclear import CC of the cyclin B1-CDK1 complex and leads to cell cycle arrest. CC {ECO:0000269|PubMed:31852787}. CC -!- INTERACTION: CC P06493; Q86V81: ALYREF; NbExp=4; IntAct=EBI-444308, EBI-347640; CC P06493; P05067: APP; NbExp=3; IntAct=EBI-444308, EBI-77613; CC P06493; O15392: BIRC5; NbExp=6; IntAct=EBI-444308, EBI-518823; CC P06493; P14635: CCNB1; NbExp=24; IntAct=EBI-444308, EBI-495332; CC P06493; P30307: CDC25C; NbExp=3; IntAct=EBI-444308, EBI-974439; CC P06493; Q99741: CDC6; NbExp=2; IntAct=EBI-444308, EBI-374862; CC P06493; P38936: CDKN1A; NbExp=7; IntAct=EBI-444308, EBI-375077; CC P06493; P46527: CDKN1B; NbExp=6; IntAct=EBI-444308, EBI-519280; CC P06493; P61024: CKS1B; NbExp=10; IntAct=EBI-444308, EBI-456371; CC P06493; O75618-1: DEDD; NbExp=2; IntAct=EBI-444308, EBI-15621191; CC P06493; P36957: DLST; NbExp=3; IntAct=EBI-444308, EBI-351007; CC P06493; P00533: EGFR; NbExp=3; IntAct=EBI-444308, EBI-297353; CC P06493; P19525: EIF2AK2; NbExp=4; IntAct=EBI-444308, EBI-640775; CC P06493; Q12778: FOXO1; NbExp=5; IntAct=EBI-444308, EBI-1108782; CC P06493; O95835: LATS1; NbExp=3; IntAct=EBI-444308, EBI-444209; CC P06493; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-444308, EBI-9090282; CC P06493; Q99640: PKMYT1; NbExp=7; IntAct=EBI-444308, EBI-495308; CC P06493; O43508: TNFSF12; NbExp=3; IntAct=EBI-444308, EBI-6932080; CC P06493; P0CG48: UBC; NbExp=6; IntAct=EBI-444308, EBI-3390054; CC P06493; P21796: VDAC1; NbExp=3; IntAct=EBI-444308, EBI-354158; CC P06493; P03070; Xeno; NbExp=2; IntAct=EBI-444308, EBI-617698; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11440}. Cytoplasm CC {ECO:0000250|UniProtKB:P11440}. Mitochondrion CC {ECO:0000269|PubMed:19917720}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, CC cytoskeleton, spindle. Note=Cytoplasmic during the interphase. CC Colocalizes with SIRT2 on centrosome during prophase and on splindle CC fibers during metaphase of the mitotic cell cycle. Reversibly CC translocated from cytoplasm to nucleus when phosphorylated before G2-M CC transition when associated with cyclin-B1. Accumulates in mitochondria CC in G2-arrested cells upon DNA-damage. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P06493-1; Sequence=Displayed; CC Name=2; Synonyms=CDC2deltaT; CC IsoId=P06493-2; Sequence=VSP_021375; CC -!- TISSUE SPECIFICITY: [Isoform 2]: Found in breast cancer tissues. CC {ECO:0000269|PubMed:9515786}. CC -!- INDUCTION: Follows a cyclic expression; during interphase, accumulates CC gradually following G1, S to reach a critical threshold at the end of CC G2, which promotes self-activation and triggers onset of mitosis. CC Induced transiently by TGFB1 at an early phase of TGFB1-mediated CC apoptosis, but later repressed. Triggered by CKS1B during mitotic entry CC in breast cancer cells. Down-regulated under genotoxic stresses CC triggered by PKR/EIF2AK2-mediated phosphorylation. CC {ECO:0000269|PubMed:17459720, ECO:0000269|PubMed:18056467}. CC -!- PTM: Phosphorylation at Thr-161 by CAK/CDK7 activates kinase activity CC (PubMed:20360007). Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 CC prevents nuclear translocation (PubMed:7569953). Phosphorylation at CC Tyr-15 by WEE1 and WEE2 inhibits the protein kinase activity and acts CC as a negative regulator of entry into mitosis (G2 to M transition) CC (PubMed:20360007). Phosphorylation by PKMYT1 and WEE1 takes place CC during mitosis to keep CDK1-cyclin-B complexes inactive until the end CC of G2 (PubMed:7569953, PubMed:20360007). By the end of G2, PKMYT1 and CC WEE1 are inactivated, but CDC25A and CDC25B are activated CC (PubMed:20360007). Dephosphorylation by active CDC25A and CDC25B at CC Thr-14 and Tyr-15, leads to CDK1 activation at the G2-M transition CC (PubMed:20360007). Phosphorylation at Tyr-15 by WEE2 during oogenesis CC is required to maintain meiotic arrest in oocytes during the germinal CC vesicle (GV) stage, a long period of quiescence at dictyate prophase I, CC leading to prevent meiotic reentry (PubMed:29606300). Phosphorylation CC by WEE2 is also required for metaphase II exit during egg activation to CC ensure exit from meiosis in oocytes and promote pronuclear formation CC (PubMed:29606300). Phosphorylated at Tyr-4 by PKR/EIF2AK2 upon CC genotoxic stress (PubMed:20395957). This phosphorylation triggers CDK1 CC polyubiquitination and subsequent proteolysis, thus leading to G2 CC arrest (PubMed:20395957). In response to UV irradiation, CC phosphorylation at Tyr-15 by PRKCD activates the G2/M DNA damage CC checkpoint (PubMed:19917613). {ECO:0000269|PubMed:19917613, CC ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:20395957, CC ECO:0000269|PubMed:29606300, ECO:0000269|PubMed:7569953}. CC -!- PTM: Polyubiquitinated upon genotoxic stress. CC {ECO:0000269|PubMed:20395957}. CC -!- MISCELLANEOUS: As a key regulator of the cell cycle, CDK1 is a potent CC therapeutic target for inhibitors in cancer treatment. CC {ECO:0000305|PubMed:21517772}. 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=EAW54204.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/cdc2/"; 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; X05360; CAA28963.1; -; mRNA. DR EMBL; Y00272; CAA68376.1; -; mRNA. DR EMBL; D88357; BAA26001.1; -; mRNA. DR EMBL; AK291939; BAF84628.1; -; mRNA. DR EMBL; BT007004; AAP35650.1; -; mRNA. DR EMBL; AF512554; AAM34793.1; -; Genomic_DNA. DR EMBL; AC022390; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471083; EAW54204.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC014563; AAH14563.1; -; mRNA. DR CCDS; CCDS44408.1; -. [P06493-1] DR CCDS; CCDS7260.1; -. [P06493-2] DR PIR; A29539; A29539. DR RefSeq; NP_001307847.1; NM_001320918.1. [P06493-1] DR RefSeq; NP_001777.1; NM_001786.4. [P06493-1] DR RefSeq; NP_203698.1; NM_033379.4. [P06493-2] DR RefSeq; XP_005270360.1; XM_005270303.3. [P06493-1] DR PDB; 4Y72; X-ray; 2.30 A; A=1-297. DR PDB; 4YC3; X-ray; 2.70 A; A=1-297. DR PDB; 4YC6; X-ray; 2.60 A; A/C/E/G=1-297. DR PDB; 5HQ0; X-ray; 2.30 A; A=1-297. DR PDB; 5LQF; X-ray; 2.06 A; A/D=1-297. DR PDB; 6GU2; X-ray; 2.00 A; A=1-297. DR PDB; 6GU3; X-ray; 2.65 A; A=1-297. DR PDB; 6GU4; X-ray; 2.73 A; A=1-297. DR PDB; 6GU6; X-ray; 2.33 A; A=1-297. DR PDB; 6GU7; X-ray; 2.75 A; A/C/E/G=1-297. DR PDB; 6TWN; X-ray; 2.28 A; C/D=207-223. DR PDB; 7NJ0; EM; 3.60 A; B=1-297. DR PDBsum; 4Y72; -. DR PDBsum; 4YC3; -. DR PDBsum; 4YC6; -. DR PDBsum; 5HQ0; -. DR PDBsum; 5LQF; -. DR PDBsum; 6GU2; -. DR PDBsum; 6GU3; -. DR PDBsum; 6GU4; -. DR PDBsum; 6GU6; -. DR PDBsum; 6GU7; -. DR PDBsum; 6TWN; -. DR PDBsum; 7NJ0; -. DR AlphaFoldDB; P06493; -. DR EMDB; EMD-12368; -. DR SMR; P06493; -. DR BioGRID; 107420; 552. DR ComplexPortal; CPX-2003; Cyclin A1-CDK1 complex. DR ComplexPortal; CPX-2004; Cyclin A2-CDK1 complex. DR ComplexPortal; CPX-2007; Cyclin B1-CDK1 complex. DR ComplexPortal; CPX-2008; Cyclin B2-CDK1 complex. DR CORUM; P06493; -. DR DIP; DIP-35N; -. DR ELM; P06493; -. DR IntAct; P06493; 204. DR MINT; P06493; -. DR STRING; 9606.ENSP00000378699; -. DR BindingDB; P06493; -. DR ChEMBL; CHEMBL308; -. DR DrugBank; DB04014; Alsterpaullone. DR DrugBank; DB03496; Alvocidib. DR DrugBank; DB08142; AT-7519. DR DrugBank; DB16652; Avotaciclib. DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB02950; Hymenialdisine. DR DrugBank; DB02052; Indirubin-3'-monoxime. DR DrugBank; DB02116; Olomoucine. DR DrugBank; DB06195; Seliciclib. DR DrugBank; DB03428; SU9516. DR DrugCentral; P06493; -. DR GuidetoPHARMACOLOGY; 1961; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyGen; P06493; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P06493; -. DR MetOSite; P06493; -. DR PhosphoSitePlus; P06493; -. DR SwissPalm; P06493; -. DR BioMuta; CDK1; -. DR DMDM; 334302921; -. DR CPTAC; CPTAC-1040; -. DR CPTAC; CPTAC-1041; -. DR CPTAC; CPTAC-1042; -. DR CPTAC; CPTAC-1200; -. DR CPTAC; CPTAC-3054; -. DR CPTAC; CPTAC-5897; -. DR CPTAC; CPTAC-5898; -. DR CPTAC; CPTAC-797; -. DR CPTAC; CPTAC-798; -. DR CPTAC; CPTAC-801; -. DR EPD; P06493; -. DR jPOST; P06493; -. DR MassIVE; P06493; -. DR MaxQB; P06493; -. DR PaxDb; 9606-ENSP00000378699; -. DR PeptideAtlas; P06493; -. DR ProteomicsDB; 51905; -. [P06493-1] DR ProteomicsDB; 51906; -. [P06493-2] DR Pumba; P06493; -. DR Antibodypedia; 1134; 2991 antibodies from 49 providers. DR CPTC; P06493; 1 antibody. DR DNASU; 983; -. DR Ensembl; ENST00000316629.8; ENSP00000325970.4; ENSG00000170312.17. [P06493-2] DR Ensembl; ENST00000373809.2; ENSP00000362915.2; ENSG00000170312.17. [P06493-2] DR Ensembl; ENST00000395284.8; ENSP00000378699.3; ENSG00000170312.17. [P06493-1] DR GeneID; 983; -. DR KEGG; hsa:983; -. DR MANE-Select; ENST00000395284.8; ENSP00000378699.3; NM_001786.5; NP_001777.1. DR UCSC; uc001jld.3; human. [P06493-1] DR AGR; HGNC:1722; -. DR CTD; 983; -. DR DisGeNET; 983; -. DR GeneCards; CDK1; -. DR HGNC; HGNC:1722; CDK1. DR HPA; ENSG00000170312; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 116940; gene. DR neXtProt; NX_P06493; -. DR OpenTargets; ENSG00000170312; -. DR PharmGKB; PA99; -. DR VEuPathDB; HostDB:ENSG00000170312; -. DR eggNOG; KOG0594; Eukaryota. DR GeneTree; ENSGT00940000153335; -. DR HOGENOM; CLU_000288_181_6_1; -. DR InParanoid; P06493; -. DR OMA; YLYQITR; -. DR OrthoDB; 244018at2759; -. DR PhylomeDB; P06493; -. DR TreeFam; TF101021; -. DR BRENDA; 2.7.11.22; 2681. DR PathwayCommons; P06493; -. DR Reactome; R-HSA-110056; MAPK3 (ERK1) activation. DR Reactome; R-HSA-113507; E2F-enabled inhibition of pre-replication complex formation. DR Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1. DR Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization. DR Reactome; R-HSA-170145; Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes. DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B. DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase. DR Reactome; R-HSA-176412; Phosphorylation of the APC/C. DR Reactome; R-HSA-176417; Phosphorylation of Emi1. DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes. DR Reactome; R-HSA-2465910; MASTL Facilitates Mitotic Progression. DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes. DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-HSA-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7. DR Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation. DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly. DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes. DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes. DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome. DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-HSA-4419969; Depolymerization of the Nuclear Lamina. DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane. DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases. DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest. DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation. DR Reactome; R-HSA-68875; Mitotic Prophase. DR Reactome; R-HSA-69205; G1/S-Specific Transcription. DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition. DR Reactome; R-HSA-69478; G2/M DNA replication checkpoint. DR Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex. DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-HSA-8854518; AURKA Activation by TPX2. DR Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2. DR Reactome; R-HSA-9833482; PKR-mediated signaling. DR SignaLink; P06493; -. DR SIGNOR; P06493; -. DR BioGRID-ORCS; 983; 864 hits in 1157 CRISPR screens. DR ChiTaRS; CDK1; human. DR GeneWiki; Cdk1; -. DR GeneWiki; Cyclin-dependent_kinase_1; -. DR GenomeRNAi; 983; -. DR Pharos; P06493; Tchem. DR PRO; PR:P06493; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P06493; Protein. DR Bgee; ENSG00000170312; Expressed in ventricular zone and 151 other cell types or tissues. DR ExpressionAtlas; P06493; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL. DR GO; GO:0097122; C:cyclin A2-CDK1 complex; ISO:ComplexPortal. DR GO; GO:0097125; C:cyclin B1-CDK1 complex; IMP:CAFA. DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:CACAO. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; TAS:UniProtKB. DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:CACAO. DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0030332; F:cyclin binding; IDA:MGI. DR GO; GO:0097472; F:cyclin-dependent protein kinase activity; IDA:UniProtKB. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0035173; F:histone kinase activity; IDA:UniProtKB. DR GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl. DR GO; GO:0016301; F:kinase activity; IDA:UniProt. DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB. 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:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IDA:UniProtKB. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0016477; P:cell migration; TAS:UniProtKB. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0007098; P:centrosome cycle; TAS:UniProtKB. DR GO; GO:0030261; P:chromosome condensation; IEA:Ensembl. DR GO; GO:0006281; P:DNA repair; TAS:UniProtKB. DR GO; GO:0006260; P:DNA replication; TAS:UniProtKB. DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; TAS:Reactome. DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0090166; P:Golgi disassembly; ISS:UniProtKB. DR GO; GO:0000226; P:microtubule cytoskeleton organization; TAS:UniProtKB. DR GO; GO:1902850; P:microtubule cytoskeleton organization involved in mitosis; IDA:UniProt. DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL. DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL. DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl. DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl. DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:CAFA. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; IMP:CAFA. DR GO; GO:0062033; P:positive regulation of mitotic sister chromatid segregation; IDA:UniProt. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB. DR GO; GO:0007344; P:pronuclear fusion; TAS:UniProtKB. DR GO; GO:0034501; P:protein localization to kinetochore; IDA:BHF-UCL. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl. DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB. DR GO; GO:0045995; P:regulation of embryonic development; TAS:UniProtKB. DR GO; GO:0014038; P:regulation of Schwann cell differentiation; TAS:UniProtKB. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0014075; P:response to amine; IEA:Ensembl. DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0046688; P:response to copper ion; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl. DR CDD; cd07861; STKc_CDK1_euk; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF334; CYCLIN-DEPENDENT KINASE 1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR SWISS-2DPAGE; P06493; -. DR Genevisible; P06493; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; ATP-binding; KW Biological rhythms; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; KW Host cell receptor for virus entry; Host-virus interaction; KW Isopeptide bond; Kinase; Mitochondrion; Mitosis; Nucleotide-binding; KW Nucleus; Phosphoprotein; Receptor; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Ubl conjugation. FT CHAIN 1..297 FT /note="Cyclin-dependent kinase 1" FT /id="PRO_0000085724" FT DOMAIN 4..287 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 128 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 10..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:22814378" FT MOD_RES 4 FT /note="Phosphotyrosine; by PKR" FT /evidence="ECO:0000269|PubMed:20395957" FT MOD_RES 6 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 9 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P11440" FT MOD_RES 14 FT /note="Phosphothreonine; by PKMYT1" FT /evidence="ECO:0000269|PubMed:7569953, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332" FT MOD_RES 15 FT /note="Phosphotyrosine; by PKMYT1, WEE1, WEE2 and FT PKC/PRKCD" FT /evidence="ECO:0000269|PubMed:19917613, FT ECO:0000269|PubMed:29606300, ECO:0000269|PubMed:7569953, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332" FT MOD_RES 19 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163" FT MOD_RES 77 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 141 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 161 FT /note="Phosphothreonine; by CAK" FT /evidence="ECO:0000269|PubMed:20360007, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 178 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES 222 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195" FT MOD_RES 245 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P11440" FT MOD_RES 248 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT CROSSLNK 6 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 9 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 20 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 139 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 107..163 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9515786" FT /id="VSP_021375" FT MUTAGEN 4 FT /note="Y->D,E: Constitutive polyubiquitination." FT /evidence="ECO:0000269|PubMed:20395957" FT MUTAGEN 14..15 FT /note="TY->AF: Abnormal cell cycle exhibiting only M-phase FT without completing either karyokinesis or cytokinesis." FT /evidence="ECO:0000269|PubMed:18480403" FT HELIX 1..3 FT /evidence="ECO:0007829|PDB:6GU2" FT STRAND 4..13 FT /evidence="ECO:0007829|PDB:6GU2" FT STRAND 16..23 FT /evidence="ECO:0007829|PDB:6GU2" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:6GU2" FT STRAND 29..35 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 46..57 FT /evidence="ECO:0007829|PDB:6GU2" FT STRAND 66..72 FT /evidence="ECO:0007829|PDB:6GU2" FT STRAND 75..81 FT /evidence="ECO:0007829|PDB:6GU2" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:5LQF" FT HELIX 87..93 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 102..120 FT /evidence="ECO:0007829|PDB:6GU2" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:6GU2" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:6GU2" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 149..152 FT /evidence="ECO:0007829|PDB:6GU6" FT STRAND 155..158 FT /evidence="ECO:0007829|PDB:6GU2" FT TURN 161..163 FT /evidence="ECO:0007829|PDB:4YC6" FT HELIX 164..167 FT /evidence="ECO:0007829|PDB:6GU6" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:6GU2" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:4YC6" FT HELIX 184..199 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 209..220 FT /evidence="ECO:0007829|PDB:6GU2" FT TURN 225..227 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 258..267 FT /evidence="ECO:0007829|PDB:6GU2" FT TURN 272..274 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 278..282 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:6GU2" FT HELIX 292..295 FT /evidence="ECO:0007829|PDB:4YC3" SQ SEQUENCE 297 AA; 34095 MW; 942D79448EFE490A CRC64; MEDYTKIEKI GEGTYGVVYK GRHKTTGQVV AMKKIRLESE EEGVPSTAIR EISLLKELRH PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQYM DSSLVKSYLY QILQGIVFCH SRRVLHRDLK PQNLLIDDKG TIKLADFGLA RAFGIPIRVY THEVVTLWYR SPEVLLGSAR YSTPVDIWSI GTIFAELATK KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNT FPKWKPGSLA SHVKNLDENG LDLLSKMLIY DPAKRISGKM ALNHPYFNDL DNQIKKM //