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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.
02-JUN-2021, entry version 224.
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 ACTIVITY
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]
INTERACTION WITH PSMA8.
PubMed=31437213; DOI=10.1371/journal.pgen.1008316;
Gomez-H L., Felipe-Medina N., Condezo Y.B., Garcia-Valiente R., Ramos I.,
Suja J.A., Barbero J.L., Roig I., Sanchez-Martin M., de Rooij D.G.,
Llano E., Pendas A.M.;
"The PSMA8 subunit of the spermatoproteasome is essential for proper
meiotic exit and mouse fertility.";
PLoS Genet. 15:E1008316-E1008316(2019).
[18]
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, TPPP, 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, SAMHD1, 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. Regulates the amplitude of the cyclic expression of the
core clock gene ARNTL/BMAL1 by phosphorylating its transcriptional
repressor NR1D1, and this phosphorylation is necessary for SCF(FBXW7)-
mediated ubiquitination and proteasomal degradation of NR1D1 (By
similarity). Phosphorylates EML3 at 'Thr-881' which is essential for
its interaction with HAUS augmin-like complex and TUBG1 (By
similarity). {ECO:0000250|UniProtKB:P06493,
ECO:0000269|PubMed:16007079, ECO:0000269|PubMed:17700700,
ECO:0000269|PubMed:17942597, ECO:0000269|PubMed:22405274}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.22;
-!- CATALYTIC ACTIVITY:
Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
ChEBI:CHEBI:456216; EC=2.7.11.23;
-!- ACTIVITY 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). Interacts with NR1D1
(By similarity). Interacts with proteasome subunit PSMA8; to
participate in meiosis progression during spermatogenesis
(PubMed:31437213). {ECO:0000250|UniProtKB:P06493,
ECO:0000269|PubMed:16007079, ECO:0000269|PubMed:17942597,
ECO:0000269|PubMed:31437213}.
-!- INTERACTION:
P11440; P51943: Ccna2; NbExp=2; IntAct=EBI-846949, EBI-846980;
P11440; Q61457: Ccne1; NbExp=3; IntAct=EBI-846949, EBI-643090;
P11440; 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.
SMR; P11440; -.
BioGRID; 198624; 137.
ComplexPortal; CPX-2061; Cyclin A1-CDK1 complex.
ComplexPortal; CPX-2062; Cyclin A2-CDK1 complex.
ComplexPortal; CPX-2069; Cyclin B1-CDK1 complex.
ComplexPortal; CPX-2070; Cyclin B2-CDK1 complex.
CORUM; P11440; -.
DIP; DIP-38725N; -.
ELM; P11440; -.
IntAct; P11440; 131.
MINT; P11440; -.
STRING; 10090.ENSMUSP00000020099; -.
BindingDB; P11440; -.
ChEMBL; CHEMBL4084; -.
iPTMnet; P11440; -.
PhosphoSitePlus; P11440; -.
SwissPalm; P11440; -.
EPD; P11440; -.
jPOST; P11440; -.
MaxQB; P11440; -.
PaxDb; P11440; -.
PeptideAtlas; P11440; -.
PRIDE; P11440; -.
ProteomicsDB; 283771; -.
Antibodypedia; 1134; 2659 antibodies.
DNASU; 12534; -.
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.
GeneTree; ENSGT00940000153335; -.
InParanoid; P11440; -.
OMA; MTHPYFD; -.
OrthoDB; 1010560at2759; -.
PhylomeDB; P11440; -.
TreeFam; TF101021; -.
BRENDA; 2.7.11.22; 3474.
Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
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-2995383; Initiation of Nuclear Envelope (NE) Reformation.
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-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-MMU-4419969; Depolymerisation of the Nuclear Lamina.
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.
Reactome; R-MMU-8878166; Transcriptional regulation by RUNX2.
BioGRID-ORCS; 12534; 21 hits in 47 CRISPR screens.
ChiTaRS; Cdk1; mouse.
PRO; PR:P11440; -.
Proteomes; UP000000589; Chromosome 10.
RNAct; P11440; protein.
Bgee; ENSMUSG00000019942; Expressed in lung and 276 other tissues.
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:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:ParkinsonsUK-UCL.
GO; GO:0106311; F:protein threonine kinase activity; IEA:RHEA.
GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; ISO:MGI.
GO; GO:0031100; P:animal organ regeneration; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007569; P:cell aging; ISO:MGI.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell population proliferation; IDA:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0030261; P:chromosome condensation; ISO:MGI.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0090166; P:Golgi disassembly; ISS:UniProtKB.
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:0010629; P:negative regulation of gene expression; 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; ISO:MGI.
GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
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; ISO:MGI.
GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; ISO:MGI.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
GO; GO:0034501; P:protein localization to kinetochore; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
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; ISO:MGI.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0010243; P:response to organonitrogen compound; ISO:MGI.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
InterPro; IPR011009; Kinase-like_dom_sf.
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; Biological rhythms; Cell cycle;
Cell division; 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
/note="Cyclin-dependent kinase 1"
/id="PRO_0000085725"
DOMAIN 4..287
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 10..18
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
ACT_SITE 128
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 33
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 4
/note="Phosphotyrosine; by PKR"
/evidence="ECO:0000250|UniProtKB:P06493"
MOD_RES 6
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 9
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 14
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:19131326,
ECO:0007744|PubMed:21183079"
MOD_RES 15
/note="Phosphotyrosine; by PKMYT1, WEE1, WEE2 and
PKC/PRKCD"
/evidence="ECO:0000305|PubMed:16169490,
ECO:0000305|PubMed:19917613, ECO:0000305|PubMed:21454751,
ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
MOD_RES 15
/note="Phosphotyrosine; by WEE1 and WEE2"
/evidence="ECO:0000269|PubMed:16169490,
ECO:0000269|PubMed:19917613, ECO:0000269|PubMed:21454751,
ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
MOD_RES 19
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P06493"
MOD_RES 39
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06493"
MOD_RES 77
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P06493"
MOD_RES 141
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P06493"
MOD_RES 161
/note="Phosphothreonine; by CAK"
/evidence="ECO:0000250|UniProtKB:P06493"
MOD_RES 178
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06493"
MOD_RES 222
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P06493"
MOD_RES 245
/note="N6-succinyllysine"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 248
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06493"
CROSSLNK 6
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P06493"
CROSSLNK 9
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P06493"
CROSSLNK 20
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P06493"
CROSSLNK 139
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P06493"
CONFLICT 112
/note="I -> M (in Ref. 4; AAB09465)"
/evidence="ECO:0000305"
CONFLICT 113
/note="L -> M (in Ref. 3; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 165
/note="V -> L (in Ref. 2; CAA34481)"
/evidence="ECO:0000305"
CONFLICT 245
/note="K -> N (in Ref. 3; AA sequence and 4; AAB09465)"
/evidence="ECO:0000305"
CONFLICT 260
/note="G -> C (in Ref. 3; AA sequence and 4; AAB09465)"
/evidence="ECO:0000305"
CONFLICT 263
/note="L -> F (in Ref. 3; AA sequence and 4; AAB09465)"
/evidence="ECO:0000305"
CONFLICT 273
/note="A -> T (in Ref. 2; CAA34481)"
/evidence="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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Related Genes :
[Cdk1 cdc2 CG5363] 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 cdcB DDB_G0272813] 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-b cdc2 cdc2x1.2] Cyclin-dependent kinase 1-B (CDK1-B) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog 2) (Cell division control protein 2-B) (Cell division protein kinase 1) (p34 protein kinase 2)
[cdk1-a cdc2-a cdc2x1.1] Cyclin-dependent kinase 1-A (CDK1-A) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog 1) (Cell division control protein 2-A) (Cell division protein kinase 1-A) (p34 protein kinase 1)
[Cdk1 Cdc2 Cdc2a Cdkn1] 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 CDC2 CDC28A CDKN1 P34CDC2] 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 Cdc2 Cdc2a Cdkn1] 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)
[cdc2 cdk1 swo2 pi002 SPBC11B10.09] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 2) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2 CDKN1] 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 CDC2 CDKN1] 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 cdc2] 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 cdc2] 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 CDC2] 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 cdc2] 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)
[nimX cdk1 AN4182] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 2) (Cell division protein kinase 1) (Never in mitosis protein X)
[CDC28 CDK1 CAALFM_CR06050WA CaO19.11337 CaO19.3856] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 28) (Cell division protein kinase 2)
[CDC28 CDK1 HSL5 SRM5 YBR160W YBR1211] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 28) (Cell division protein kinase 1)
[cdk1 cdc2] 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 cdc2] 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)
[CDKA-1 CDC2 CDC2A At3g48750 T21J18.20] Cyclin-dependent kinase A-1 (CDKA;1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog A) (CDC2aAt)
[CDK7 CAK CAK1 CDKN7 MO15 STK1] Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 kDa protein kinase) (p39 Mo15) (CDK-activating kinase 1) (Cell division protein kinase 7) (Serine/threonine-protein kinase 1) (TFIIH basal transcription factor complex kinase subunit)
[CDK2 CDKN2] Cyclin-dependent kinase 2 (EC 2.7.11.22) (Cell division protein kinase 2) (p33 protein kinase)
[CDKB1-1 CDC2B At3g54180 F24B22.140] Cyclin-dependent kinase B1-1 (CDKB1;1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog B)
[Cdk7 Cak Cak1 Mo15] Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 protein kinase) (P39 Mo15) (CDK-activating kinase 1) (Cell division protein kinase 7) (TFIIH basal transcription factor complex kinase subunit) (Fragment)
[Cdk7 Cak Cdkn7 Crk4 Mo15 Mpk-7] Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 kDa protein kinase) (P39 Mo15) (CDK-activating kinase) (CR4 protein kinase) (CRK4) (Cell division protein kinase 7) (Protein-tyrosine kinase MPK-7) (TFIIH basal transcription factor complex kinase subunit)
[CDK9 CDC2L4 TAK] Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)
[Cdk11b Cdc2l1 Cdk11] Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1)
[CDK13 CDC2L CDC2L5 CHED KIAA1791] Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller)
[CDC2] Cell division control protein 2 homolog (EC 2.7.11.22) (EC 2.7.11.23) (p34cdc2)
[CDK11B CDC2L1 CDK11 PITSLREA PK58] Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)

Bibliography :
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