Cdk1
entrez
54237
canonical
uniprot
P39951
canonical
ensembl
ENSRNOG00000000632
resolver
ensembl
ENSRNOG00055021827
resolver
ensembl
ENSRNOG00060028733
resolver
ensembl
ENSRNOG00065027158
resolver
ensp
ENSRNOP00000072365
resolver
ensp
ENSRNOP00055030518
resolver
ensp
ENSRNOP00060041662
resolver
ensp
ENSRNOP00065038400
resolver
enst
ENSRNOT00000086806
resolver
enst
ENSRNOT00055037434
resolver
enst
ENSRNOT00060049974
resolver
enst
ENSRNOT00065046823
resolver
genesymbol
Cdk1
resolver
genesymbol_syn
Cdc2
resolver
genesymbol_syn
Cdc2a
resolver
genesymbol_syn
Cdkn1
resolver
uniprot
Q5BJB4
resolver
uniprot_entry
CDK1_RAT
resolver
uniprot_sec
Q5BJB4
resolver
activity_regulation
ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-161 activates it (By similarity). Binding to cyclin-B is required for relocation of cyclin-kinase complexes to the nucleus for activation (By similarity). Activated by CAK/CDK7-mediated phosphorylation on Thr-161, and reciprocally phosphorylates its activating kinase CDK7 (By similarity). CDC25-mediated dephosphorylation of inhibitory phosphorylation on Thr-14 and Tyr-15 is required for full activation (By similarity). Activity is restricted during S-phase in an ATR-dependent manner to prevent premature entry into G2 (By similarity). 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:0000250|UniProtKB:P06493}.
uniprot
proteins
amino_acid_sequence
MEDYIKIEKIGEGTYGVVYKGRHRTTGQIVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQFMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLVYDPAKRISGKMALKHPYFDDLDNQIKKM
uniprot
proteins
ec_number
2.7.11.22
uniprot
proteins
ec_number
2.7.11.23
uniprot
proteins
function
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 via association with multiple interphase cyclins (PubMed:10542199, PubMed:19821535). Phosphorylates PARVA/actopaxin, APC, AMPH, APC, ASB7, 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, UHRF1, KAT5, LMNA, LMNB, LBR, MKI67, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MLST8, 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, RBBP8/CtIP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SAMHD1, SIRT2, CGAS, GLI2, ZAR1 and RUNX2 (PubMed:10542199, PubMed:19821535). CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs (By similarity). Essential for early stages of embryonic development (By similarity). 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 (By similarity). 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 (By similarity). Phosphorylates KRT5 during prometaphase and metaphase (By similarity). Activated by the CDK-activating kinase (CAK) complex consisting of CDK7, cyclin-H/CCNH and MAT1, which is a master regulator of CDK activity (By similarity). 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 (By similarity). Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C-mediated dephosphorylation and restoring cell cycle progression (By similarity). Catalyzes lamin (LMNA, LMNB1 and LMNB2) phosphorylation at the onset of mitosis, promoting nuclear envelope breakdown (By similarity). 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 (By similarity). The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis (By similarity). 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 (By similarity). In addition, CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis (By similarity). The phosphorylation of Bcl-xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis (By similarity). In contrast, CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis (By similarity). This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes (By similarity). EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing (By similarity). CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration (PubMed:17200138). CDK1-cyclin-B complex phosphorylates NCKAP5L and mediates its dissociation from centrosomes during mitosis (By similarity). Regulates the amplitude of the cyclic expression of the core clock gene 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). Phosphorylates CGAS during mitosis, leading to its inhibition, thereby preventing CGAS activation by self DNA during mitosis (By similarity). Phosphorylates SKA3 during mitosis which promotes SKA3 binding to the NDC80 complex and anchoring of the SKA complex to kinetochores, to enable stable attachment of mitotic spindle microtubules to kinetochores (By similarity). {ECO:0000250|UniProtKB:P06493, ECO:0000250|UniProtKB:P11440, ECO:0000269|PubMed:10542199, ECO:0000269|PubMed:17200138, ECO:0000269|PubMed:19821535}.
uniprot
proteins
mass_dalton
34135
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-161 by CAK/CDK7 activates kinase activity (By similarity). Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents nuclear translocation (By similarity). 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) (By similarity). Phosphorylation by PKMYT1 and WEE1 takes place during mitosis to keep CDK1-cyclin-B complexes inactive until the end of G2 (By similarity). By the end of G2, PKMYT1 and WEE1 are inactivated, but CDC25A and CDC25B are activated (By similarity). Dephosphorylation by active CDC25A and CDC25B at Thr-14 and Tyr-15, leads to CDK1 activation at the G2-M transition (By similarity). 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 (By similarity). Phosphorylation by WEE2 is also required for metaphase II exit during egg activation to ensure exit from meiosis in oocytes and promote pronuclear formation (By similarity). Phosphorylated at Tyr-4 by PKR/EIF2AK2 upon genotoxic stress (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P06493}.; PTM: Polyubiquitinated upon genotoxic stress (By similarity). {ECO:0000250|UniProtKB:P06493}.
uniprot
proteins
protein_family
CDC2/CDKX subfamily
uniprot
proteins
protein_family
CMGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10542199
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17200138
uniprot
proteins
pubmed
19821535
uniprot
proteins
pubmed
2541912
uniprot
proteins
sequence_length
297
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19821535, ECO:0000269|PubMed:2541912}. Cytoplasm {ECO:0000250|UniProtKB:P11440}. Mitochondrion {ECO:0000250|UniProtKB:P11440}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P06493}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P06493}. 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|UniProtKB:P06493}.
uniprot
proteins