ID CDK1_RAT Reviewed; 297 AA.
AC P39951; Q5BJB4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 194.
DE RecName: Full=Cyclin-dependent kinase 1;
DE Short=CDK1;
DE EC=2.7.11.22 {ECO:0000250|UniProtKB:P06493};
DE EC=2.7.11.23 {ECO:0000250|UniProtKB:P11440};
DE AltName: Full=Cell division control protein 2 homolog;
DE AltName: Full=Cell division protein kinase 1;
DE AltName: Full=p34 protein kinase;
GN Name=Cdk1; Synonyms=Cdc2, Cdc2a, Cdkn1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kanaoka Y., Nojima H., Okayama H.;
RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=2541912; DOI=10.1016/0092-8674(89)90914-8;
RA Riabowol K., Draetta G., Brizuela L., Vandre D., Beach D.;
RT "The cdc2 kinase is a nuclear protein that is essential for mitosis in
RT mammalian cells.";
RL Cell 57:393-401(1989).
RN [4]
RP FUNCTION AS RB1 KINASE, INDUCTION BY TGFB1, AND INTERACTION WITH RB1.
RX PubMed=10542199; DOI=10.1074/jbc.274.45.31775;
RA Choi K.S., Eom Y.W., Kang Y., Ha M.J., Rhee H., Yoon J.-W., Kim S.-J.;
RT "Cdc2 and Cdk2 kinase activated by transforming growth factor-beta1 trigger
RT apoptosis through the phosphorylation of retinoblastoma protein in FaO
RT hepatoma cells.";
RL J. Biol. Chem. 274:31775-31783(1999).
RN [5]
RP FUNCTION AS CALD1 KINASE.
RX PubMed=17200138; DOI=10.1242/jcs.03322;
RA Han I.S., Seo T.B., Kim K.-H., Yoon J.-H., Yoon S.-J., Namgung U.;
RT "Cdc2-mediated Schwann cell migration during peripheral nerve
RT regeneration.";
RL J. Cell Sci. 120:246-255(2007).
RN [6]
RP FUNCTION, INTERACTION WITH CYCLIN-A AND B1, INDUCTION BY MITOGEN AGENT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19821535; DOI=10.1002/hep.23225;
RA Garnier D., Loyer P., Ribault C., Guguen-Guillouzo C., Corlu A.;
RT "Cyclin-dependent kinase 1 plays a critical role in DNA replication control
RT during rat liver regeneration.";
RL Hepatology 50:1946-1956(2009).
CC -!- FUNCTION: Plays a key role in the control of the eukaryotic cell cycle
CC by modulating the centrosome cycle as well as mitotic onset; promotes
CC G2-M transition via association with multiple interphase cyclins
CC (PubMed:10542199, PubMed:19821535). Phosphorylates PARVA/actopaxin,
CC APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20,
CC CDC25A, CDC25C, CC2D1A, CENPA, CSNK2 proteins/CKII, FZR1/CDH1, CDK7,
CC CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5,
CC EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1
CC proteins/histone H1, HMGA1, HIVEP3/KRC, KAT5, LMNA, LMNB, LBR, LATS1,
CC MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MLST8, MYB, NEFH, NFIC,
CC NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1,
CC NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53,
CC NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, TPPP, UL40/R2, RAB4A, RAP1GAP,
CC RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1,
CC TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1,
CC RUNX1/AML1, SAMHD1, SIRT2, CGAS, ZAR1 and RUNX2 (PubMed:10542199,
CC PubMed:19821535). CDK1/CDC2-cyclin-B controls pronuclear union in
CC interphase fertilized eggs (By similarity). Essential for early stages
CC of embryonic development (By similarity). During G2 and early mitosis,
CC CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes
CC which phosphorylate several substrates that trigger at least centrosome
CC separation, Golgi dynamics, nuclear envelope breakdown and chromosome
CC condensation (By similarity). Once chromosomes are condensed and
CC aligned at the metaphase plate, CDK1 activity is switched off by
CC WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid
CC separation, chromosome decondensation, reformation of the nuclear
CC envelope and cytokinesis (By similarity). Phosphorylates KRT5 during
CC prometaphase and metaphase (By similarity). Inactivated by
CC PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop
CC cell cycle and genome replication at the G2 checkpoint thus
CC facilitating DNA repair (By similarity). Reactivated after successful
CC DNA repair through WIP1-dependent signaling leading to CDC25A/B/C-
CC mediated dephosphorylation and restoring cell cycle progression (By
CC similarity). Catalyzes lamin (LMNA, LMNB1 and LMNB2) phosphorylation at
CC the onset of mitosis, promoting nuclear envelope breakdown (By
CC similarity). In proliferating cells, CDK1-mediated FOXO1
CC phosphorylation at the G2-M phase represses FOXO1 interaction with 14-
CC 3-3 proteins and thereby promotes FOXO1 nuclear accumulation and
CC transcription factor activity, leading to cell death of postmitotic
CC neurons (By similarity). The phosphorylation of beta-tubulins regulates
CC microtubule dynamics during mitosis (By similarity). NEDD1
CC phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and
CC subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the
CC centrosome, an important step for spindle formation (By similarity). In
CC addition, CC2D1A phosphorylation regulates CC2D1A spindle pole
CC localization and association with SCC1/RAD21 and centriole cohesion
CC during mitosis (By similarity). The phosphorylation of Bcl-xL/BCL2L1
CC after prolongated G2 arrest upon DNA damage triggers apoptosis (By
CC similarity). In contrast, CASP8 phosphorylation during mitosis prevents
CC its activation by proteolysis and subsequent apoptosis (By similarity).
CC This phosphorylation occurs in cancer cell lines, as well as in primary
CC breast tissues and lymphocytes (By similarity). EZH2 phosphorylation
CC promotes H3K27me3 maintenance and epigenetic gene silencing (By
CC similarity). CALD1 phosphorylation promotes Schwann cell migration
CC during peripheral nerve regeneration (PubMed:17200138). CDK1-cyclin-B
CC complex phosphorylates NCKAP5L and mediates its dissociation from
CC centrosomes during mitosis (By similarity). Regulates the amplitude of
CC the cyclic expression of the core clock gene BMAL1 by phosphorylating
CC its transcriptional repressor NR1D1, and this phosphorylation is
CC necessary for SCF(FBXW7)-mediated ubiquitination and proteasomal
CC degradation of NR1D1 (By similarity). Phosphorylates EML3 at 'Thr-881'
CC which is essential for its interaction with HAUS augmin-like complex
CC and TUBG1 (By similarity). Phosphorylates CGAS during mitosis, leading
CC to its inhibition, thereby preventing CGAS activation by self DNA
CC during mitosis (By similarity). {ECO:0000250|UniProtKB:P06493,
CC ECO:0000250|UniProtKB:P11440, ECO:0000269|PubMed:10542199,
CC ECO:0000269|PubMed:17200138, ECO:0000269|PubMed:19821535}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC Evidence={ECO:0000250|UniProtKB:P06493};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P06493};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC Evidence={ECO:0000250|UniProtKB:P11440};
CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC the enzyme, while phosphorylation at Thr-161 activates it. Activated
CC through a multistep process; binding to cyclin-B is required for
CC relocation of cyclin-kinase complexes to the nucleus, activated by
CC CAK/CDK7-mediated phosphorylation on Thr-161, and CDC25-mediated
CC dephosphorylation of inhibitory phosphorylation on Thr-14 and Tyr-15.
CC Activity is restricted during S-phase in an ATR-dependent manner to
CC prevent premature entry into G2. Repressed by the CDK inhibitors
CC CDKN1A/p21 and CDKN1B/p27 during the G1 phase and by CDKN1A/p21 at the
CC G1-S checkpoint upon DNA damage. Transient activation by rapid and
CC transient dephosphorylation at Tyr-15 triggered by TGFB1.
CC {ECO:0000250|UniProtKB:P06493}.
CC -!- SUBUNIT: Forms a stable but non-covalent complex with a regulatory
CC subunit and with a cyclin. Interacts with cyclins-B (CCNB1, CCNB2 and
CC CCNB3) to form a serine/threonine kinase holoenzyme complex also known
CC as maturation promoting factor (MPF). The cyclin subunit imparts
CC substrate specificity to the complex. Can also form CDK1-cylin-D and
CC CDK1-cyclin-E complexes that phosphorylate RB1 in vitro. Binds to RB1
CC and other transcription factors such as FOXO1 and RUNX2. Promotes G2-M
CC transition when in complex with a cyclin-B. Interacts with DLGAP5.
CC Binds to the CDK inhibitors CDKN1A/p21 and CDKN1B/p27. Isoform 2 is
CC unable to complex with cyclin-B1 and also fails to bind to CDKN1A/p21.
CC Interacts with catalytically active CCNB1 and RALBP1 during mitosis to
CC form an endocytotic complex during interphase. Associates with cyclins-
CC A and B1 during S-phase in regenerating hepatocytes. Interacts with
CC FANCC. Interacts with CEP63; this interaction recruits CDK1 to
CC centrosomes. Interacts with CENPA. Interacts with NR1D1 (By
CC similarity). Interacts with proteasome subunit PSMA8; to participate in
CC meiosis progression during spermatogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P06493, ECO:0000250|UniProtKB:P11440,
CC ECO:0000269|PubMed:10542199, ECO:0000269|PubMed:19821535}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19821535,
CC ECO:0000269|PubMed:2541912}. Cytoplasm {ECO:0000250|UniProtKB:P11440}.
CC Mitochondrion {ECO:0000250|UniProtKB:P11440}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P06493}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P06493}. Note=Colocalizes with SIRT2 on
CC centrosome during prophase and on splindle fibers during metaphase of
CC the mitotic cell cycle (By similarity). Cytoplasmic during the
CC interphase. Reversibly translocated from cytoplasm to nucleus when
CC phosphorylated before G2-M transition when associated with cyclin-B1.
CC Accumulates in mitochondria in G2-arrested cells upon DNA-damage.
CC {ECO:0000250|UniProtKB:P06493}.
CC -!- INDUCTION: Follow a cyclic expression; during interphase, accumulates
CC gradually following G1, S to reach a critical threshold at the end of
CC G2, which promotes self-activation and triggers onset of mitosis.
CC Induced transiently by TGFB1 at an early phase of TGFB1-mediated
CC apoptosis. Expressed during S-phase in mitogen-stimulated hepatocytes.
CC {ECO:0000269|PubMed:10542199, ECO:0000269|PubMed:19821535}.
CC -!- PTM: Phosphorylation at Thr-161 by CAK/CDK7 activates kinase activity.
CC Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents nuclear
CC translocation. Phosphorylation at Tyr-15 by WEE1 and WEE2 inhibits the
CC protein kinase activity and acts as a negative regulator of entry into
CC mitosis (G2 to M transition). Phosphorylation by PKMYT1 and WEE1 takes
CC place during mitosis to keep CDK1-cyclin-B complexes inactive until the
CC end of G2. By the end of G2, PKMYT1 and WEE1 are inactivated, but
CC CDC25A and CDC25B are activated. Dephosphorylation by active CDC25A and
CC CDC25B at Thr-14 and Tyr-15, leads to CDK1 activation at the G2-M
CC transition. Phosphorylation at Tyr-15 by WEE2 during oogenesis is
CC required to maintain meiotic arrest in oocytes during the germinal
CC vesicle (GV) stage, a long period of quiescence at dictyate prophase I,
CC leading to prevent meiotic reentry. Phosphorylation by WEE2 is also
CC required for metaphase II exit during egg activation to ensure exit
CC from meiosis in oocytes and promote pronuclear formation.
CC Phosphorylated at Tyr-4 by PKR/EIF2AK2 upon genotoxic stress. This
CC phosphorylation triggers CDK1 polyubiquitination and subsequent
CC proteolysis, thus leading to G2 arrest. In response to UV irradiation,
CC phosphorylation at Tyr-15 by PRKCD activates the G2/M DNA damage
CC checkpoint (By similarity). {ECO:0000250|UniProtKB:P06493}.
CC -!- PTM: Polyubiquitinated upon genotoxic stress.
CC {ECO:0000250|UniProtKB:P06493}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; X60767; CAA43177.1; -; mRNA.
DR EMBL; BC091549; AAH91549.1; -; mRNA.
DR PIR; S24913; S24913.
DR RefSeq; NP_062169.1; NM_019296.1.
DR RefSeq; XP_006256415.1; XM_006256353.3.
DR AlphaFoldDB; P39951; -.
DR SMR; P39951; -.
DR BioGRID; 248460; 3.
DR ComplexPortal; CPX-2063; Cyclin A1-CDK1 complex.
DR ComplexPortal; CPX-2064; Cyclin A2-CDK1 complex.
DR ComplexPortal; CPX-2072; Cyclin B1-CDK1 complex.
DR CORUM; P39951; -.
DR IntAct; P39951; 2.
DR STRING; 10116.ENSRNOP00000070138; -.
DR iPTMnet; P39951; -.
DR PhosphoSitePlus; P39951; -.
DR jPOST; P39951; -.
DR PaxDb; 10116-ENSRNOP00000000783; -.
DR Ensembl; ENSRNOT00000086806.2; ENSRNOP00000072365.1; ENSRNOG00000000632.7.
DR Ensembl; ENSRNOT00055037434; ENSRNOP00055030518; ENSRNOG00055021827.
DR Ensembl; ENSRNOT00060049974; ENSRNOP00060041662; ENSRNOG00060028733.
DR Ensembl; ENSRNOT00065046823; ENSRNOP00065038400; ENSRNOG00065027158.
DR GeneID; 54237; -.
DR KEGG; rno:54237; -.
DR UCSC; RGD:2319; rat.
DR AGR; RGD:2319; -.
DR CTD; 983; -.
DR RGD; 2319; Cdk1.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000153335; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P39951; -.
DR OMA; YLYQITR; -.
DR OrthoDB; 244018at2759; -.
DR PhylomeDB; P39951; -.
DR TreeFam; TF101021; -.
DR BRENDA; 2.7.11.22; 5301.
DR Reactome; R-RNO-110056; MAPK3 (ERK1) activation.
DR Reactome; R-RNO-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-RNO-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-RNO-176412; Phosphorylation of the APC/C.
DR Reactome; R-RNO-176417; Phosphorylation of Emi1.
DR Reactome; R-RNO-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
DR Reactome; R-RNO-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-4419969; Depolymerization of the Nuclear Lamina.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-5689896; Ovarian tumor domain proteases.
DR Reactome; R-RNO-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-RNO-68875; Mitotic Prophase.
DR Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-RNO-69478; G2/M DNA replication checkpoint.
DR Reactome; R-RNO-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR Reactome; R-RNO-9833482; PKR-mediated signaling.
DR PRO; PR:P39951; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000632; Expressed in thymus and 17 other cell types or tissues.
DR Genevisible; P39951; RN.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0097122; C:cyclin A2-CDK1 complex; ISO:RGD.
DR GO; GO:0097125; C:cyclin B1-CDK1 complex; ISO:RGD.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; ISO:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0030332; F:cyclin binding; IPI:RGD.
DR GO; GO:0097472; F:cyclin-dependent protein kinase activity; ISO:RGD.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0035173; F:histone kinase activity; IDA:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IMP:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:RGD.
DR GO; GO:0030261; P:chromosome condensation; IMP:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0048144; P:fibroblast proliferation; ISO:RGD.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0090166; P:Golgi disassembly; IDA:UniProtKB.
DR GO; GO:1902850; P:microtubule cytoskeleton organization involved in mitosis; ISO:RGD.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; ISO:RGD.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:RGD.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; ISO:RGD.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:RGD.
DR GO; GO:0062033; P:positive regulation of mitotic sister chromatid segregation; ISO:RGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:0034501; P:protein localization to kinetochore; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0014075; P:response to amine; IEP:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IDA:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IDA:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IEP:RGD.
DR CDD; cd07861; STKc_CDK1_euk; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR PANTHER; PTHR24056:SF334; CYCLIN-DEPENDENT KINASE 1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; ATP-binding; Biological rhythms; Cell cycle;
KW Cell division; Cytoplasm; Cytoskeleton; Isopeptide bond; Kinase;
KW Mitochondrion; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT CHAIN 1..297
FT /note="Cyclin-dependent kinase 1"
FT /id="PRO_0000085727"
FT DOMAIN 4..287
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 4
FT /note="Phosphotyrosine; by PKR"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 9
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11440"
FT MOD_RES 14
FT /note="Phosphothreonine; by PKMYT1"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 15
FT /note="Phosphotyrosine; by PKMYT1, WEE1, WEE2 and
FT PKC/PRKCD"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 15
FT /note="Phosphotyrosine; by WEE1 and WEE2"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 19
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 77
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 161
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT MOD_RES 245
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11440"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT CROSSLNK 9
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P06493"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P06493"
SQ SEQUENCE 297 AA; 34135 MW; 73695017E127178A CRC64;
MEDYIKIEKI GEGTYGVVYK GRHRTTGQIV AMKKIRLESE EEGVPSTAIR EISLLKELRH
PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQFM DSSLVKSYLY QILQGIVFCH
SRRVLHRDLK PQNLLIDDKG TIKLADFGLA RAFGIPIRVY THEVVTLWYR SPEVLLGSAR
YSTPVDIWSI GTIFAELATK KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNT
FPKWKPGSLA SHVKNLDENG LDLLSKMLVY DPAKRISGKM ALKHPYFDDL DNQIKKM
//
