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Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)

 CDK1_HUMAN              Reviewed;         297 AA.
P06493; A8K7C4; C9J497; O60764;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
31-MAY-2011, sequence version 3.
27-SEP-2017, entry version 225.
RecName: Full=Cyclin-dependent kinase 1;
Short=CDK1;
EC=2.7.11.22;
EC=2.7.11.23;
AltName: Full=Cell division control protein 2 homolog;
AltName: Full=Cell division protein kinase 1;
AltName: Full=p34 protein kinase;
Name=CDK1; Synonyms=CDC2, CDC28A, CDKN1, P34CDC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3553962; DOI=10.1038/327031a0;
Lee M.G., Nurse P.;
"Complementation used to clone a human homologue of the fission yeast
cell cycle control gene cdc2.";
Nature 327:31-35(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Mammary cancer;
PubMed=9515786;
Ohta T., Okamoto K., Isohashi F., Shibata K., Fukuda M., Yamaguchi S.,
Xiong Y.;
"T-loop deletion of CDC2 from breast cancer tissues eliminates binding
to cyclin B1 and cyclin-dependent kinase inhibitor p21.";
Cancer Res. 58:1095-1098(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PHOSPHORYLATION, AND ASSOCIATION WITH P13.
PubMed=3289755; DOI=10.1016/0092-8674(88)90175-4;
Draetta G., Beach D.;
"Activation of cdc2 protein kinase during mitosis in human cells: cell
cycle-dependent phosphorylation and subunit rearrangement.";
Cell 54:17-26(1988).
[10]
PHOSPHORYLATION AT THR-14 AND TYR-15 BY PKMYT1.
PubMed=7569953; DOI=10.1126/science.270.5233.86;
Mueller P.R., Coleman T.R., Kumagai A., Dunphy W.G.;
"Myt1: a membrane-associated inhibitory kinase that phosphorylates
Cdc2 on both threonine-14 and tyrosine-15.";
Science 270:86-90(1995).
[11]
INTERACTION WITH FANCC.
PubMed=9242535;
Kupfer G.M., Yamashita T., Naf D., Suliman A., Asano S.,
D'Andrea A.D.;
"The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent
kinase, cdc2.";
Blood 90:1047-1054(1997).
[12]
ENZYME REGULATION BY ROSCOVITINE AND OLOMOUCINE.
PubMed=9030781; DOI=10.1111/j.1432-1033.1997.t01-2-00527.x;
Meijer L., Borgne A., Mulner O., Chong J.P.J., Blow J.J., Inagaki N.,
Inagaki M., Delcros J.-G., Moulinoux J.-P.;
"Biochemical and cellular effects of roscovitine, a potent and
selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and
cdk5.";
Eur. J. Biochem. 243:527-536(1997).
[13]
INTERACTION WITH RALBP1.
PubMed=12775724; DOI=10.1074/jbc.M302191200;
Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.;
"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to
phosphorylate epsin during the switch off of endocytosis in mitosis.";
J. Biol. Chem. 278:30597-30604(2003).
[14]
INTERACTION WITH DLGAP5.
PubMed=15145941; DOI=10.1074/jbc.M404950200;
Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.;
"Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-
phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a
proline-rich region.";
J. Biol. Chem. 279:32592-32602(2004).
[15]
FUNCTION AS RUNX2 KINASE.
PubMed=16407259; DOI=10.1074/jbc.M508162200;
Qiao M., Shapiro P., Fosbrink M., Rus H., Kumar R., Passaniti A.;
"Cell cycle-dependent phosphorylation of the RUNX2 transcription
factor by cdc2 regulates endothelial cell proliferation.";
J. Biol. Chem. 281:7118-7128(2006).
[16]
FUNCTION AS BETA-TUBULINS KINASE.
PubMed=16371510; DOI=10.1091/mbc.E05-07-0621;
Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I.,
Juillan-Binard C., Lantez V., Job D.;
"Microtubule regulation in mitosis: tubulin phosphorylation by the
cyclin-dependent kinase Cdk1.";
Mol. Biol. Cell 17:1041-1050(2006).
[17]
INDUCTION BY CKS1B.
PubMed=18056467; DOI=10.1158/0008-5472.CAN-06-4173;
Westbrook L., Manuvakhova M., Kern F.G., Estes N.R. II,
Ramanathan H.N., Thottassery J.V.;
"Cks1 regulates cdk1 expression: a novel role during mitotic entry in
breast cancer cells.";
Cancer Res. 67:11393-11401(2007).
[18]
FUNCTION AS RB1 KINASE, ENZYME REGULATION BY TGFB1, AND REPRESSION BY
TGFB1.
PubMed=17459720; DOI=10.1016/j.cyto.2007.03.009;
Hu X., Cui D., Moscinski L.C., Zhang X., Maccachero V.,
Zuckerman K.S.;
"TGFbeta regulates the expression and activities of G2 checkpoint
kinases in human myeloid leukemia cells.";
Cytokine 37:155-162(2007).
[19]
FUNCTION AS SIRT2 KINASE, AND SUBCELLULAR LOCATION.
PubMed=16933150; DOI=10.1007/s11064-006-9127-6;
Southwood C.M., Peppi M., Dryden S., Tainsky M.A., Gow A.;
"Microtubule deacetylases, SirT2 and HDAC6, in the nervous system.";
Neurochem. Res. 32:187-195(2007).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[21]
FUNCTION DURING THE M PHASE, AND MUTAGENESIS OF 14-THR-TYR-15.
PubMed=18480403; DOI=10.1091/mbc.E08-02-0172;
Pomerening J.R., Ubersax J.A., Ferrell J.E. Jr.;
"Rapid cycling and precocious termination of G1 phase in cells
expressing CDK1AF.";
Mol. Biol. Cell 19:3426-3441(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19; SER-39; TYR-77 AND
THR-222, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
FUNCTION AS FOXO1 KINASE, AND INTERACTION WITH FOXO1.
PubMed=18356527; DOI=10.1126/science.1152337;
Yuan Z., Becker E.B.E., Merlo P., Yamada T., DiBacco S., Konishi Y.,
Schaefer E.M., Bonni A.;
"Activation of FOXO1 by Cdk1 in cycling cells and postmitotic
neurons.";
Science 319:1665-1668(2008).
[25]
FUNCTION AS NEDD1 KINASE.
PubMed=19509060; DOI=10.1242/jcs.042747;
Zhang X., Chen Q., Feng J., Hou J., Yang F., Liu J., Jiang Q.,
Zhang C.;
"Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for
targeting of the gammaTuRC to the centrosome.";
J. Cell Sci. 122:2240-2251(2009).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT TYR-19; SER-39; SER-178; THR-222 AND SER-248, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15 AND THR-161,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[29]
FUNCTION AS CC2D1A KINASE.
PubMed=20171170; DOI=10.1016/j.bbrc.2010.02.103;
Nakamura A., Naito M., Arai H., Fujita N.;
"Mitotic phosphorylation of Aki1 at Ser208 by cyclin B1-Cdk1
complex.";
Biochem. Biophys. Res. Commun. 393:872-876(2010).
[30]
FUNCTION IN G2 ARREST UPON DNA DAMAGE, PHOSPHORYLATION AT TYR-4 BY
PKR/EIF2AK2, POLYUBIQUITINATION, AND MUTAGENESIS OF TYR-4.
PubMed=20395957; DOI=10.1038/embor.2010.45;
Yoon C.-H., Miah M.A., Kim K.P., Bae Y.-S.;
"New Cdc2 Tyr 4 phosphorylation by dsRNA-activated protein kinase
triggers Cdc2 polyubiquitination and G2 arrest under genotoxic
stresses.";
EMBO Rep. 11:393-399(2010).
[31]
PHOSPHORYLATION AT TYR-15.
PubMed=19917613; DOI=10.1074/jbc.M109.055392;
LaGory E.L., Sitailo L.A., Denning M.F.;
"The protein kinase Cdelta catalytic fragment is critical for
maintenance of the G2/M DNA damage checkpoint.";
J. Biol. Chem. 285:1879-1887(2010).
[32]
FUNCTION IN G2-M TRANSITION, DEPHOSPHORYLATION AT THR-14 AND TYR-15 BY
CDC25, PHOSPHORYLATION AT THR-161 BY CDK7/CAK, AND INTERACTION WITH
B-CYCLIN.
PubMed=20360007; DOI=10.1074/jbc.M109.096552;
Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.;
"Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B
at the G2/M transition.";
J. Biol. Chem. 285:16978-16990(2010).
[33]
FUNCTION AS BCL-XL/BCL2L1 KINASE, AND SUBCELLULAR LOCATION.
PubMed=19917720; DOI=10.1128/MCB.00882-09;
Terrano D.T., Upreti M., Chambers T.C.;
"Cyclin-dependent kinase 1-mediated Bcl-xL/Bcl-2 phosphorylation acts
as a functional link coupling mitotic arrest and apoptosis.";
Mol. Cell. Biol. 30:640-656(2010).
[34]
FUNCTION AS CASP8 KINASE.
PubMed=20937773; DOI=10.1128/MCB.00731-10;
Matthess Y., Raab M., Sanhaji M., Lavrik I.N., Strebhardt K.;
"Cdk1/cyclin B1 controls Fas-mediated apoptosis by regulating caspase-
8 activity.";
Mol. Cell. Biol. 30:5726-5740(2010).
[35]
FUNCTION AS EZH2 KINASE.
PubMed=20935635; DOI=10.1038/ncb2116;
Chen S., Bohrer L.R., Rai A.N., Pan Y., Gan L., Zhou X., Bagchi A.,
Simon J.A., Huang H.;
"Cyclin-dependent kinases regulate epigenetic gene silencing through
phosphorylation of EZH2.";
Nat. Cell Biol. 12:1108-1114(2010).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[38]
INTERACTION WITH CEP63, AND SUBCELLULAR LOCATION.
PubMed=21406398; DOI=10.1158/0008-5472.CAN-10-2684;
Loffler H., Fechter A., Matuszewska M., Saffrich R., Mistrik M.,
Marhold J., Hornung C., Westermann F., Bartek J., Kramer A.;
"Cep63 recruits Cdk1 to the centrosome: implications for regulation of
mitotic entry, centrosome amplification, and genome maintenance.";
Cancer Res. 71:2129-2139(2011).
[39]
FUNCTION AS CHAMP1 KINASE.
PubMed=21063390; DOI=10.1038/emboj.2010.276;
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K.,
Mizuno K., Yasui A., Hirota T., Tanaka K.;
"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-
microtubule attachment.";
EMBO J. 30:130-144(2011).
[40]
REVIEW ON SUBSTRATES, AND GENE FAMILY.
PubMed=16236519; DOI=10.1016/j.tibs.2005.09.005;
Malumbres M., Barbacid M.;
"Mammalian cyclin-dependent kinases.";
Trends Biochem. Sci. 30:630-641(2005).
[41]
REVIEW ON SUBCELLULAR TRANSLOCATION.
PubMed=19364923; DOI=10.1083/jcb.200812045;
Lindqvist A., Rodriguez-Bravo V., Medema R.H.;
"The decision to enter mitosis: feedback and redundancy in the mitotic
entry network.";
J. Cell Biol. 185:193-202(2009).
[42]
REVIEW ON CELL CYCLE CONTROL AND INHIBITORS, AND GENE FAMILY.
PubMed=19238148; DOI=10.1038/nrc2602;
Malumbres M., Barbacid M.;
"Cell cycle, CDKs and cancer: a changing paradigm.";
Nat. Rev. Cancer 9:153-166(2009).
[43]
REVIEW ON CELL CYCLE CONTROL.
PubMed=21535261; DOI=10.1111/j.1365-2184.2011.00753.x;
Hu X., Moscinski L.C.;
"Cdc2: a monopotent or pluripotent CDK?";
Cell Prolif. 44:205-211(2011).
[44]
REVIEW ON CELL CYCLE CONTROL AND INHIBITORS.
PubMed=21517772; DOI=10.2174/092986711795590110;
Wang Q., Su L., Liu N., Zhang L., Xu W., Fang H.;
"Cyclin dependent kinase 1 inhibitors: a review of recent progress.";
Curr. Med. Chem. 18:2025-2043(2011).
[45]
REVIEW ON CELL CYCLE CONTROL.
PubMed=21655336; DOI=10.3410/B3-10;
Medema R.H., Macurek L.;
"Checkpoint recovery in cells: how a molecular understanding can help
in the fight against cancer.";
F1000 Biol. Rep. 3:10-10(2011).
[46]
FUNCTION (MICROBIAL INFECTION).
PubMed=21516087; DOI=10.1038/nm.2341;
Lupberger J., Zeisel M.B., Xiao F., Thumann C., Fofana I., Zona L.,
Davis C., Mee C.J., Turek M., Gorke S., Royer C., Fischer B.,
Zahid M.N., Lavillette D., Fresquet J., Cosset F.L., Rothenberg S.M.,
Pietschmann T., Patel A.H., Pessaux P., Doffoel M., Raffelsberger W.,
Poch O., McKeating J.A., Brino L., Baumert T.F.;
"EGFR and EphA2 are host factors for hepatitis C virus entry and
possible targets for antiviral therapy.";
Nat. Med. 17:589-595(2011).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[48]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[49]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; THR-141 AND THR-161,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[50]
FUNCTION.
PubMed=26549230; DOI=10.1016/j.bbrc.2015.11.004;
Mori Y., Inoue Y., Taniyama Y., Tanaka S., Terada Y.;
"Phosphorylation of the centrosomal protein, Cep169, by Cdk1 promotes
its dissociation from centrosomes in mitosis.";
Biochem. Biophys. Res. Commun. 468:642-646(2015).
[51]
FUNCTION, AND INTERACTION WITH CENPA.
PubMed=25556658; DOI=10.1016/j.devcel.2014.11.030;
Yu Z., Zhou X., Wang W., Deng W., Fang J., Hu H., Wang Z., Li S.,
Cui L., Shen J., Zhai L., Peng S., Wong J., Dong S., Yuan Z., Ou G.,
Zhang X., Xu P., Lou J., Yang N., Chen P., Xu R.M., Li G.;
"Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-
cycle-dependent deposition at centromeres.";
Dev. Cell 32:68-81(2015).
[52]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[53]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-20 AND
LYS-139, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Plays a key role in the control of the eukaryotic cell
cycle by modulating the centrosome cycle as well as mitotic onset;
promotes G2-M transition, and regulates G1 progress and G1-S
transition via association with multiple interphase cyclins.
Required in higher cells for entry into S-phase and mitosis.
Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-
xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C,
CC2D1A, CENPA, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB,
CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR,
FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1
proteins/histone H1, HMGA1, HIVEP3/KRC, LMNA, LMNB, LMNC, LBR,
LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MYB, NEFH, NFIC,
NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1,
NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53,
NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, UL40/R2, RAB4A, RAP1GAP,
RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin,
STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1,
FOXO1, RUNX1/AML1, SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls
pronuclear union in interphase fertilized eggs. Essential for
early stages of embryonic development. During G2 and early
mitosis, CDC25A/B/C-mediated dephosphorylation activates
CDK1/cyclin complexes which phosphorylate several substrates that
trigger at least centrosome separation, Golgi dynamics, nuclear
envelope breakdown and chromosome condensation. Once chromosomes
are condensed and aligned at the metaphase plate, CDK1 activity is
switched off by WEE1- and PKMYT1-mediated phosphorylation to allow
sister chromatid separation, chromosome decondensation,
reformation of the nuclear envelope and cytokinesis. Inactivated
by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage
to stop cell cycle and genome replication at the G2 checkpoint
thus facilitating DNA repair. Reactivated after successful DNA
repair through WIP1-dependent signaling leading to CDC25A/B/C-
mediated dephosphorylation and restoring cell cycle progression.
In proliferating cells, CDK1-mediated FOXO1 phosphorylation at the
G2-M phase represses FOXO1 interaction with 14-3-3 proteins and
thereby promotes FOXO1 nuclear accumulation and transcription
factor activity, leading to cell death of postmitotic neurons. The
phosphorylation of beta-tubulins regulates microtubule dynamics
during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1
phosphorylation and subsequent targeting of the gamma-tubulin ring
complex (gTuRC) to the centrosome, an important step for spindle
formation. In addition, CC2D1A phosphorylation regulates CC2D1A
spindle pole localization and association with SCC1/RAD21 and
centriole cohesion during mitosis. The phosphorylation of Bcl-
xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers
apoptosis. In contrast, CASP8 phosphorylation during mitosis
prevents its activation by proteolysis and subsequent apoptosis.
This phosphorylation occurs in cancer cell lines, as well as in
primary breast tissues and lymphocytes. EZH2 phosphorylation
promotes H3K27me3 maintenance and epigenetic gene silencing. CALD1
phosphorylation promotes Schwann cell migration during peripheral
nerve regeneration. CDK1-cyclin-B complex phosphorylates NCKAP5L
and mediates its dissociation from centrosomes during mitosis
(PubMed:26549230). {ECO:0000269|PubMed:16371510,
ECO:0000269|PubMed:16407259, ECO:0000269|PubMed:16933150,
ECO:0000269|PubMed:17459720, ECO:0000269|PubMed:18356527,
ECO:0000269|PubMed:18480403, ECO:0000269|PubMed:19509060,
ECO:0000269|PubMed:19917720, ECO:0000269|PubMed:20171170,
ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:20395957,
ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:20937773,
ECO:0000269|PubMed:21063390, ECO:0000269|PubMed:25556658,
ECO:0000269|PubMed:26549230}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C
virus (HCV) in hepatocytes and facilitates its cell entry.
{ECO:0000269|PubMed:21516087}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
[DNA-directed RNA polymerase] phosphate.
-!- ENZYME REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
the enzyme, while phosphorylation at Thr-161 activates it.
Activated through a multistep process; binding to cyclin-B is
required for relocation of cyclin-kinase complexes to the nucleus,
activated by CAK/CDK7-mediated phosphorylation on Thr-161, and
CDC25-mediated dephosphorylation of inhibitory phosphorylation on
Thr-14 and Tyr-15. Inhibited by flavopiridol and derivatives,
pyrimidine derivatives, pyridine derivatives, purine derivatives,
staurosporine, paullones, oxoindoles, indazole analogs, indolin-2-
ones, pyrazolo[3,4-b]pyridines, imidazo[1,2-a]pyridine (AZ703),
thiazolinone analogs(RO-3306), thiazol urea, macrocyclic
quinoxalin-2-one, pyrrolo[2,3-a]carbazole, pyrazolo[1,5-a]-1,3,5-
triazine, pyrazolo[1,5-a]pyrimidine (Dinaciclib, SCH 727965), 2-
(1-ethyl-2-hydroxyethylamino)-6-benzylamino-9-isopropylpurine
(roscovitine), olomoucine, AG-024322, AT-7519, P276-00, R547/Ro-
4584820 and SNS-032/BMS-387032. Repressed by the CDK inhibitors
CDKN1A/p21 and CDKN1B/p27 during the G1 phase and by CDKN1A/p21 at
the G1-S checkpoint upon DNA damage. Transient activation by rapid
and transient dephosphorylation at Tyr-15 triggered by TGFB1.
{ECO:0000269|PubMed:17459720, ECO:0000269|PubMed:9030781}.
-!- SUBUNIT: Forms a stable but non-covalent complex with a regulatory
subunit and with a cyclin. Interacts with cyclins-B (CCNB1, CCNB2
and CCNB3) to form a serine/threonine kinase holoenzyme complex
also known as maturation promoting factor (MPF). The cyclin
subunit imparts substrate specificity to the complex. Can also
form CDK1-cylin-D and CDK1-cyclin-E complexes that phosphorylate
RB1 in vitro. Binds to RB1 and other transcription factors such as
FOXO1 and RUNX2. Promotes G2-M transition when in complex with a
cyclin-B. Interacts with DLGAP5. Binds to the CDK inhibitors
CDKN1A/p21 and CDKN1B/p27. Isoform 2 is unable to complex with
cyclin-B1 and also fails to bind to CDKN1A/p21. Interacts with
catalytically active CCNB1 and RALBP1 during mitosis to form an
endocytotic complex during interphase. Associates with cyclins-A
and B1 during S-phase in regenerating hepatocytes. Interacts with
FANCC. Interacts with CEP63; this interaction recruits CDK1 to
centrosomes. Interacts with CENPA (PubMed:25556658).
{ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:15145941,
ECO:0000269|PubMed:18356527, ECO:0000269|PubMed:20360007,
ECO:0000269|PubMed:21406398, ECO:0000269|PubMed:25556658,
ECO:0000269|PubMed:9242535}.
-!- INTERACTION:
P03070:- (xeno); NbExp=2; IntAct=EBI-444308, EBI-617698;
O15392:BIRC5; NbExp=6; IntAct=EBI-444308, EBI-518823;
P14635:CCNB1; NbExp=10; IntAct=EBI-444308, EBI-495332;
P30307:CDC25C; NbExp=2; IntAct=EBI-444308, EBI-974439;
P38936:CDKN1A; NbExp=3; IntAct=EBI-444308, EBI-375077;
P61024:CKS1B; NbExp=8; IntAct=EBI-444308, EBI-456371;
P19525:EIF2AK2; NbExp=4; IntAct=EBI-444308, EBI-640775;
Q12778:FOXO1; NbExp=5; IntAct=EBI-444308, EBI-1108782;
O95835:LATS1; NbExp=2; IntAct=EBI-444308, EBI-444209;
Q99640:PKMYT1; NbExp=4; IntAct=EBI-444308, EBI-495308;
P0CG48:UBC; NbExp=6; IntAct=EBI-444308, EBI-3390054;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion.
Cytoplasm, cytoskeleton, microtubule organizing center,
centrosome. Cytoplasm, cytoskeleton, spindle. Note=Cytoplasmic
during the interphase. Colocalizes with SIRT2 on centrosome during
prophase and on splindle fibers during metaphase of the mitotic
cell cycle. Reversibly translocated from cytoplasm to nucleus when
phosphorylated before G2-M transition when associated with cyclin-
B1. Accumulates in mitochondria in G2-arrested cells upon DNA-
damage.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P06493-1; Sequence=Displayed;
Name=2; Synonyms=CDC2deltaT;
IsoId=P06493-2; Sequence=VSP_021375;
-!- TISSUE SPECIFICITY: Isoform 2 is found in breast cancer tissues.
-!- INDUCTION: Follows a cyclic expression; during interphase,
accumulates gradually following G1, S to reach a critical
threshold at the end of G2, which promotes self-activation and
triggers onset of mitosis. Induced transiently by TGFB1 at an
early phase of TGFB1-mediated apoptosis, but later repressed.
Triggered by CKS1B during mitotic entry in breast cancer cells.
Down-regulated under genotoxic stresses triggered by PKR/EIF2AK2-
mediated phosphorylation. {ECO:0000269|PubMed:17459720,
ECO:0000269|PubMed:18056467}.
-!- PTM: Phosphorylation at Thr-161 by CAK/CDK7 activates kinase
activity. Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents
nuclear translocation. Phosphorylation at Tyr-15 by WEE1 and WEE2
inhibits the protein kinase activity and acts as a negative
regulator of entry into mitosis (G2 to M transition).
Phosphorylation by PKMYT1 and WEE1 takes place during mitosis to
keep CDK1-cyclin-B complexes inactive until the end of G2. By the
end of G2, PKMYT1 and WEE1 are inactivated, but CDC25A and CDC25B
are activated. Dephosphorylation by active CDC25A and CDC25B at
Thr-14 and Tyr-15, leads to CDK1 activation at the G2-M
transition. Phosphorylation at Tyr-15 by WEE2 during oogenesis is
required to maintain meiotic arrest in oocytes during the germinal
vesicle (GV) stage, a long period of quiescence at dictyate
prophase I, leading to prevent meiotic reentry. Phosphorylation by
WEE2 is also required for metaphase II exit during egg activation
to ensure exit from meiosis in oocytes and promote pronuclear
formation. Phosphorylated at Tyr-4 by PKR/EIF2AK2 upon genotoxic
stress. This phosphorylation triggers CDK1 polyubiquitination and
subsequent proteolysis, thus leading to G2 arrest. In response to
UV irradiation, phosphorylation at Tyr-15 by PRKCD activates the
G2/M DNA damage checkpoint. {ECO:0000269|PubMed:19917613,
ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:20395957,
ECO:0000269|PubMed:3289755, ECO:0000269|PubMed:7569953}.
-!- PTM: Polyubiquitinated upon genotoxic stress.
{ECO:0000269|PubMed:20395957}.
-!- MISCELLANEOUS: As a key regulator of the cell cycle, CDK1 is a
potent therapeutic target for inhibitors in cancer treatment.
{ECO:0000305|PubMed:21517772}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EAW54204.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc2/";
-----------------------------------------------------------------------
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EMBL; X05360; CAA28963.1; -; mRNA.
EMBL; Y00272; CAA68376.1; -; mRNA.
EMBL; D88357; BAA26001.1; -; mRNA.
EMBL; AK291939; BAF84628.1; -; mRNA.
EMBL; BT007004; AAP35650.1; -; mRNA.
EMBL; AF512554; AAM34793.1; -; Genomic_DNA.
EMBL; AC022390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54204.1; ALT_SEQ; Genomic_DNA.
EMBL; BC014563; AAH14563.1; -; mRNA.
CCDS; CCDS44408.1; -. [P06493-1]
CCDS; CCDS7260.1; -. [P06493-2]
PIR; A29539; A29539.
RefSeq; NP_001307847.1; NM_001320918.1. [P06493-1]
RefSeq; NP_001777.1; NM_001786.4. [P06493-1]
RefSeq; NP_203698.1; NM_033379.4. [P06493-2]
RefSeq; XP_005270360.1; XM_005270303.3. [P06493-1]
UniGene; Hs.732435; -.
PDB; 1LC9; Model; -; A=1-297.
PDB; 4Y72; X-ray; 2.30 A; A=1-297.
PDB; 4YC3; X-ray; 2.70 A; A=1-297.
PDB; 4YC6; X-ray; 2.60 A; A/C/E/G=1-297.
PDB; 5HQ0; X-ray; 2.30 A; A=1-297.
PDB; 5LQF; X-ray; 2.06 A; A/D=1-297.
PDBsum; 1LC9; -.
PDBsum; 4Y72; -.
PDBsum; 4YC3; -.
PDBsum; 4YC6; -.
PDBsum; 5HQ0; -.
PDBsum; 5LQF; -.
ProteinModelPortal; P06493; -.
SMR; P06493; -.
BioGrid; 107420; 219.
CORUM; P06493; -.
DIP; DIP-35N; -.
ELM; P06493; -.
IntAct; P06493; 98.
MINT; MINT-5000894; -.
STRING; 9606.ENSP00000378699; -.
BindingDB; P06493; -.
ChEMBL; CHEMBL308; -.
DrugBank; DB04014; Alsterpaullone.
DrugBank; DB05037; AT7519.
DrugBank; DB03496; Flavopiridol.
DrugBank; DB02950; Hymenialdisine.
DrugBank; DB02052; Indirubin-3'-Monoxime.
DrugBank; DB02116; Olomoucine.
DrugBank; DB03428; SU9516.
GuidetoPHARMACOLOGY; 1961; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; P06493; -.
PhosphoSitePlus; P06493; -.
SwissPalm; P06493; -.
BioMuta; CDK1; -.
DMDM; 334302921; -.
SWISS-2DPAGE; P06493; -.
EPD; P06493; -.
MaxQB; P06493; -.
PaxDb; P06493; -.
PeptideAtlas; P06493; -.
PRIDE; P06493; -.
DNASU; 983; -.
Ensembl; ENST00000316629; ENSP00000325970; ENSG00000170312. [P06493-2]
Ensembl; ENST00000373809; ENSP00000362915; ENSG00000170312. [P06493-2]
Ensembl; ENST00000395284; ENSP00000378699; ENSG00000170312. [P06493-1]
GeneID; 983; -.
KEGG; hsa:983; -.
UCSC; uc001jld.3; human. [P06493-1]
CTD; 983; -.
DisGeNET; 983; -.
EuPathDB; HostDB:ENSG00000170312.15; -.
GeneCards; CDK1; -.
HGNC; HGNC:1722; CDK1.
HPA; CAB003799; -.
HPA; HPA003387; -.
MIM; 116940; gene.
neXtProt; NX_P06493; -.
OpenTargets; ENSG00000170312; -.
PharmGKB; PA99; -.
eggNOG; KOG0594; Eukaryota.
eggNOG; ENOG410XPP3; LUCA.
GeneTree; ENSGT00890000139329; -.
HOVERGEN; HBG014652; -.
InParanoid; P06493; -.
KO; K02087; -.
OMA; EMMLVYD; -.
PhylomeDB; P06493; -.
TreeFam; TF101021; -.
BRENDA; 2.7.11.22; 2681.
Reactome; R-HSA-110056; MAPK3 (ERK1) activation.
Reactome; R-HSA-113507; E2F-enabled inhibition of pre-replication complex formation.
Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
Reactome; R-HSA-170145; Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-HSA-176412; Phosphorylation of the APC/C.
Reactome; R-HSA-176417; Phosphorylation of Emi1.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-2465910; MASTL Facilitates Mitotic Progression.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-68875; Mitotic Prophase.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-69478; G2/M DNA replication checkpoint.
Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SignaLink; P06493; -.
SIGNOR; P06493; -.
ChiTaRS; CDK1; human.
GeneWiki; Cdk1; -.
GeneWiki; Cyclin-dependent_kinase_1; -.
GenomeRNAi; 983; -.
PRO; PR:P06493; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000170312; -.
CleanEx; HS_CDC2; -.
ExpressionAtlas; P06493; baseline and differential.
Genevisible; P06493; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0097125; C:cyclin B1-CDK1 complex; IMP:CAFA.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; TAS:UniProtKB.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0030332; F:cyclin binding; IDA:MGI.
GO; GO:0097472; F:cyclin-dependent protein kinase activity; IDA:UniProtKB.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0035173; F:histone kinase activity; IDA:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IDA:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007569; P:cell aging; IEA:Ensembl.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; TAS:UniProtKB.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0007098; P:centrosome cycle; TAS:UniProtKB.
GO; GO:0030261; P:chromosome condensation; IEA:Ensembl.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0006281; P:DNA repair; TAS:UniProtKB.
GO; GO:0006260; P:DNA replication; TAS:UniProtKB.
GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0090166; P:Golgi disassembly; ISS:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; TAS:UniProtKB.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IEA:Ensembl.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:CAFA.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; IMP:CAFA.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0007344; P:pronuclear fusion; TAS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0006461; P:protein complex assembly; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0034501; P:protein localization to kinetochore; IDA:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IMP:CAFA.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0045995; P:regulation of embryonic development; TAS:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0051445; P:regulation of meiotic cell cycle; IBA:GO_Central.
GO; GO:0014038; P:regulation of Schwann cell differentiation; TAS:UniProtKB.
GO; GO:0051439; P:regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0014075; P:response to amine; IEA:Ensembl.
GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Cell cycle; Cell division; Complete proteome; Cytoplasm;
Cytoskeleton; Host cell receptor for virus entry; Isopeptide bond;
Kinase; Mitochondrion; Mitosis; Nucleotide-binding; Nucleus;
Phosphoprotein; Receptor; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 297 Cyclin-dependent kinase 1.
/FTId=PRO_0000085724.
DOMAIN 4 287 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 10 18 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 128 128 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 33 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:22814378}.
MOD_RES 4 4 Phosphotyrosine; by PKR.
{ECO:0000269|PubMed:20395957}.
MOD_RES 6 6 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 9 9 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P11440}.
MOD_RES 14 14 Phosphothreonine; by PKMYT1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:7569953}.
MOD_RES 15 15 Phosphotyrosine; by PKMYT1, WEE1, WEE2
and PKC/PRKCD.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:19917613,
ECO:0000269|PubMed:7569953}.
MOD_RES 19 19 Phosphotyrosine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 77 77 Phosphotyrosine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 141 141 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 161 161 Phosphothreonine; by CAK.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:20360007}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 222 222 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 245 245 N6-succinyllysine.
{ECO:0000250|UniProtKB:P11440}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 9 9 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 20 20 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 139 139 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 107 163 Missing (in isoform 2).
{ECO:0000303|PubMed:9515786}.
/FTId=VSP_021375.
MUTAGEN 4 4 Y->D,E: Constitutive polyubiquitination.
{ECO:0000269|PubMed:20395957}.
MUTAGEN 14 15 TY->AF: Abnormal cell cycle exhibiting
only M-phase without completing either
karyokinesis or cytokinesis.
{ECO:0000269|PubMed:18480403}.
HELIX 1 3 {ECO:0000244|PDB:5LQF}.
STRAND 4 12 {ECO:0000244|PDB:5LQF}.
STRAND 17 23 {ECO:0000244|PDB:5LQF}.
TURN 24 26 {ECO:0000244|PDB:5LQF}.
STRAND 29 34 {ECO:0000244|PDB:5LQF}.
HELIX 40 42 {ECO:0000244|PDB:5LQF}.
HELIX 46 57 {ECO:0000244|PDB:5LQF}.
STRAND 66 72 {ECO:0000244|PDB:5LQF}.
STRAND 75 81 {ECO:0000244|PDB:5LQF}.
STRAND 84 86 {ECO:0000244|PDB:5LQF}.
HELIX 87 92 {ECO:0000244|PDB:5LQF}.
HELIX 102 120 {ECO:0000244|PDB:5LQF}.
TURN 121 123 {ECO:0000244|PDB:5LQF}.
HELIX 131 133 {ECO:0000244|PDB:5LQF}.
STRAND 134 136 {ECO:0000244|PDB:5LQF}.
STRAND 142 144 {ECO:0000244|PDB:5LQF}.
HELIX 149 152 {ECO:0000244|PDB:4YC6}.
STRAND 155 157 {ECO:0000244|PDB:5LQF}.
TURN 161 163 {ECO:0000244|PDB:4YC6}.
HELIX 166 169 {ECO:0000244|PDB:4YC6}.
HELIX 172 175 {ECO:0000244|PDB:5LQF}.
STRAND 179 181 {ECO:0000244|PDB:4YC6}.
HELIX 184 199 {ECO:0000244|PDB:5LQF}.
HELIX 209 220 {ECO:0000244|PDB:5LQF}.
TURN 225 227 {ECO:0000244|PDB:5LQF}.
HELIX 231 233 {ECO:0000244|PDB:5LQF}.
HELIX 249 251 {ECO:0000244|PDB:5LQF}.
HELIX 258 267 {ECO:0000244|PDB:5LQF}.
TURN 272 274 {ECO:0000244|PDB:5LQF}.
HELIX 278 281 {ECO:0000244|PDB:5LQF}.
HELIX 285 288 {ECO:0000244|PDB:5LQF}.
HELIX 292 295 {ECO:0000244|PDB:4YC3}.
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


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