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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_MOUSE              Reviewed;         297 AA.
P11440; P70337; Q3TI12;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 3.
25-OCT-2017, entry version 196.
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, Cdc2a, Cdkn1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=FM3A; TISSUE=Mammary carcinoma;
PubMed=2208288; DOI=10.1016/0092-8674(90)90164-A;
Th'Ng J.P.H., Wright P.S., Hamaguchi J., Lee M.G., Norbury C.J.,
Nurse P., Bradbury E.M.;
"The FT210 cell line is a mouse G2 phase mutant with a temperature-
sensitive CDC2 gene product.";
Cell 63:313-324(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=2132958; DOI=10.3109/10425179009041346;
Spurr N.K., Gough A.C., Lee M.G.;
"Cloning of the mouse homologue of the yeast cell cycle control gene
cdc2.";
DNA Seq. 1:49-54(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2662013; DOI=10.1038/339679a0;
Cisek L.J., Corden J.L.;
"Phosphorylation of RNA polymerase by the murine homologue of the
cell-cycle control protein cdc2.";
Nature 339:679-684(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=9895127;
Jun D., Park H.K., Nordin A.A., Nagel J.E., Kim Y.H.;
"Characterization of the murine cdc2 gene.";
Mol. Cells 8:731-740(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Muellerian duct, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[7]
PHOSPHORYLATION AT TYR-15.
PubMed=16169490; DOI=10.1016/j.cub.2005.07.056;
Han S.J., Chen R., Paronetto M.P., Conti M.;
"Wee1B is an oocyte-specific kinase involved in the control of meiotic
arrest in the mouse.";
Curr. Biol. 15:1670-1676(2005).
[8]
FUNCTION AT THE TRANSITION G1-S, INTERACTION WITH CDKN1B/P27 AND
CYCLIN E1, AND REGULATION BY CDKN1B/P27.
PubMed=16007079; DOI=10.1038/ncb1284;
Aleem E., Kiyokawa H., Kaldis P.;
"Cdc2-cyclin E complexes regulate the G1/S phase transition.";
Nat. Cell Biol. 7:831-836(2005).
[9]
FUNCTION IN CELL CYCLE REGULATION, AND DISRUPTION PHENOTYPE.
PubMed=17700700; DOI=10.1038/nature06046;
Santamaria D., Barriere C., Cerqueira A., Hunt S., Tardy C.,
Newton K., Caceres J.F., Dubus P., Malumbres M., Barbacid M.;
"Cdk1 is sufficient to drive the mammalian cell cycle.";
Nature 448:811-815(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
FUNCTION, INTERACTION WITH CDKN1A/P21, SUBCELLULAR LOCATION, AND
ENZYME REGULATION BY CDKN1A/P21.
PubMed=17942597; DOI=10.1091/mbc.E07-06-0525;
Satyanarayana A., Hilton M.B., Kaldis P.;
"p21 Inhibits Cdk1 in the absence of Cdk2 to maintain the G1/S phase
DNA damage checkpoint.";
Mol. Biol. Cell 19:65-77(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
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).
[15]
PHOSPHORYLATION AT TYR-15.
PubMed=21454751; DOI=10.1126/science.1199211;
Oh J.S., Susor A., Conti M.;
"Protein tyrosine kinase Wee1B is essential for metaphase II exit in
mouse oocytes.";
Science 332:462-465(2011).
[16]
FUNCTION IN PHOSPHORYLATION OF TEX14.
PubMed=22405274; DOI=10.1016/j.molcel.2012.01.013;
Mondal G., Ohashi A., Yang L., Rowley M., Couch F.J.;
"Tex14, a plk1-regulated protein, is required for kinetochore-
microtubule attachment and regulation of the spindle assembly
checkpoint.";
Mol. Cell 45:680-695(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-6 AND LYS-9,
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-245, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- 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.
{ECO:0000250|UniProtKB:P06493, ECO:0000269|PubMed:16007079,
ECO:0000269|PubMed:17700700, ECO:0000269|PubMed:17942597,
ECO:0000269|PubMed:22405274}.
-!- 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.
{ECO:0000250}.
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:P06493, ECO:0000269|PubMed:16007079,
ECO:0000269|PubMed:17942597}.
-!- INTERACTION:
P51943:Ccna2; NbExp=2; IntAct=EBI-846949, EBI-846980;
Q61457:Ccne1; NbExp=3; IntAct=EBI-846949, EBI-643090;
P20263:Pou5f1; NbExp=4; IntAct=EBI-846949, EBI-1606219;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17942597}.
Cytoplasm {ECO:0000269|PubMed:17942597}. Mitochondrion
{ECO:0000269|PubMed:17942597}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome {ECO:0000250}.
Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Colocalizes
with SIRT2 on centrosome during prophase and on splindle fibers
during metaphase of the mitotic cell cycle (By similarity).
Cytoplasmic during the interphase. 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. {ECO:0000250}.
-!- INDUCTION: Follow 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 (Probable). {ECO:0000305}.
-!- 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 (By similarity).
In response to UV irradiation, phosphorylation at Tyr-15 by PRKCD
activates the G2/M DNA damage checkpoint. {ECO:0000250,
ECO:0000269|PubMed:16169490, ECO:0000269|PubMed:19917613,
ECO:0000269|PubMed:21454751}.
-!- PTM: Polyubiquitinated upon genotoxic stress.
{ECO:0000250|UniProtKB:P06493}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality in the first cell
divisions. {ECO:0000269|PubMed:17700700}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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EMBL; M38724; AAA37408.1; -; mRNA.
EMBL; X16461; CAA34481.1; -; mRNA.
EMBL; U58633; AAB09465.1; -; mRNA.
EMBL; AK030231; BAC26856.1; -; mRNA.
EMBL; AK135516; BAE22561.1; -; mRNA.
EMBL; AK168054; BAE40034.1; -; mRNA.
EMBL; BC024396; AAH24396.1; -; mRNA.
CCDS; CCDS23908.1; -.
PIR; A36074; A36074.
RefSeq; NP_031685.2; NM_007659.3.
UniGene; Mm.281367; -.
ProteinModelPortal; P11440; -.
SMR; P11440; -.
BioGrid; 198624; 133.
CORUM; P11440; -.
DIP; DIP-38725N; -.
ELM; P11440; -.
IntAct; P11440; 127.
MINT; MINT-4587254; -.
STRING; 10090.ENSMUSP00000020099; -.
BindingDB; P11440; -.
ChEMBL; CHEMBL4084; -.
iPTMnet; P11440; -.
PhosphoSitePlus; P11440; -.
EPD; P11440; -.
MaxQB; P11440; -.
PaxDb; P11440; -.
PeptideAtlas; P11440; -.
PRIDE; P11440; -.
Ensembl; ENSMUST00000020099; ENSMUSP00000020099; ENSMUSG00000019942.
Ensembl; ENSMUST00000119827; ENSMUSP00000113184; ENSMUSG00000019942.
GeneID; 12534; -.
KEGG; mmu:12534; -.
UCSC; uc007fmr.1; mouse.
CTD; 983; -.
MGI; MGI:88351; Cdk1.
eggNOG; KOG0594; Eukaryota.
eggNOG; ENOG410XPP3; LUCA.
GeneTree; ENSGT00900000140881; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P11440; -.
KO; K02087; -.
OMA; EMMLVYD; -.
OrthoDB; EOG091G0CH0; -.
PhylomeDB; P11440; -.
TreeFam; TF101021; -.
BRENDA; 2.7.11.22; 3474.
Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
Reactome; R-MMU-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-MMU-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-MMU-176412; Phosphorylation of the APC/C.
Reactome; R-MMU-176417; Phosphorylation of Emi1.
Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-MMU-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-MMU-4419969; Depolymerisation of the Nuclear Lamina.
Reactome; R-MMU-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
Reactome; R-MMU-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
Reactome; R-MMU-68875; Mitotic Prophase.
Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-MMU-69478; G2/M DNA replication checkpoint.
Reactome; R-MMU-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-MMU-8854518; AURKA Activation by TPX2.
PRO; PR:P11440; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000019942; -.
CleanEx; MM_CDC2A; -.
ExpressionAtlas; P11440; baseline and differential.
Genevisible; P11440; MM.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0097125; C:cyclin B1-CDK1 complex; ISO:MGI.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005876; C:spindle microtubule; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0030332; F:cyclin binding; ISO:MGI.
GO; GO:0097472; F:cyclin-dependent protein kinase activity; ISO:MGI.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0035173; F:histone kinase activity; ISO:MGI.
GO; GO:0030544; F:Hsp70 protein binding; IPI:MGI.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0004672; F:protein kinase activity; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:ParkinsonsUK-UCL.
GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; ISO:MGI.
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:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IDA:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0030261; P:chromosome condensation; IEA:Ensembl.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
GO; GO:0090166; P:Golgi disassembly; ISS:UniProtKB.
GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
GO; GO:0044772; P:mitotic cell cycle phase transition; IMP:MGI.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IDA:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS: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; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; ISO:MGI.
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; ISO:MGI.
GO; GO:0006461; P:protein complex assembly; IEA:Ensembl.
GO; GO:0034501; P:protein localization to kinetochore; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
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:0000083; P:regulation of transcription involved in G1/S transition of 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;
Acetylation; Apoptosis; ATP-binding; Cell cycle; Cell division;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Isopeptide bond; Kinase; Mitochondrion; Mitosis; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 297 Cyclin-dependent kinase 1.
/FTId=PRO_0000085725.
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:23806337}.
MOD_RES 4 4 Phosphotyrosine; by PKR.
{ECO:0000250|UniProtKB:P06493}.
MOD_RES 6 6 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 9 9 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 14 14 Phosphothreonine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 15 15 Phosphotyrosine; by PKMYT1, WEE1, WEE2
and PKC/PRKCD.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079,
ECO:0000305|PubMed:16169490,
ECO:0000305|PubMed:19917613,
ECO:0000305|PubMed:21454751}.
MOD_RES 15 15 Phosphotyrosine; by WEE1 and WEE2.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:16169490,
ECO:0000269|PubMed:19917613,
ECO:0000269|PubMed:21454751}.
MOD_RES 19 19 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06493}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:P06493}.
MOD_RES 77 77 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06493}.
MOD_RES 141 141 Phosphothreonine.
{ECO:0000250|UniProtKB:P06493}.
MOD_RES 161 161 Phosphothreonine; by CAK.
{ECO:0000250|UniProtKB:P06493}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000250|UniProtKB:P06493}.
MOD_RES 222 222 Phosphothreonine.
{ECO:0000250|UniProtKB:P06493}.
MOD_RES 245 245 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000250|UniProtKB:P06493}.
CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06493}.
CROSSLNK 9 9 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06493}.
CROSSLNK 20 20 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P06493}.
CROSSLNK 139 139 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P06493}.
CONFLICT 112 112 I -> M (in Ref. 4; AAB09465).
{ECO:0000305}.
CONFLICT 113 113 L -> M (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 165 165 V -> L (in Ref. 2; CAA34481).
{ECO:0000305}.
CONFLICT 245 245 K -> N (in Ref. 3; AA sequence and 4;
AAB09465). {ECO:0000305}.
CONFLICT 260 260 G -> C (in Ref. 3; AA sequence and 4;
AAB09465). {ECO:0000305}.
CONFLICT 263 263 L -> F (in Ref. 3; AA sequence and 4;
AAB09465). {ECO:0000305}.
CONFLICT 273 273 A -> T (in Ref. 2; CAA34481).
{ECO:0000305}.
SEQUENCE 297 AA; 34107 MW; 9C399FCC41BA7F31 CRC64;
MEDYIKIEKI GEGTYGVVYK GRHRVTGQIV AMKKIRLESE EEGVPSTAIR EISLLKELRH
PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQFM DSSLVKSYLH QILQGIVFCH
SRRVLHRDLK PQNLLIDDKG TIKLADFGLA RAFGIPIRVY THEVVTLWYR SPEVLLGSAR
YSTPVDIWSI GTIFAELATK KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNT
FPKWKPGSLA SHVKNLDENG LDLLSKMLVY DPAKRISGKM ALKHPYFDDL DNQIKKM


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