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P11440

- CDK1_MOUSE

UniProt

P11440 - CDK1_MOUSE

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Protein

Cyclin-dependent kinase 1

Gene

Cdk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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, 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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Enzyme regulationi

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-161 activates it.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATPPROSITE-ProRule annotation
Active sitei128 – 1281Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  3. histone kinase activity Source: Ensembl
  4. Hsp70 protein binding Source: MGI
  5. kinase activity Source: MGI
  6. protein serine/threonine kinase activity Source: ParkinsonsUK-UCL
  7. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell aging Source: Ensembl
  3. cellular response to hydrogen peroxide Source: Ensembl
  4. chromosome condensation Source: Ensembl
  5. epithelial cell differentiation Source: Ensembl
  6. mitotic G2 DNA damage checkpoint Source: MGI
  7. mitotic nuclear division Source: UniProtKB-KW
  8. negative regulation of apoptotic process Source: Ensembl
  9. organ regeneration Source: Ensembl
  10. peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
  11. peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCL
  12. positive regulation of cardiac muscle cell proliferation Source: Ensembl
  13. positive regulation of DNA replication Source: Ensembl
  14. positive regulation of gene expression Source: Ensembl
  15. positive regulation of mitotic cell cycle Source: Ensembl
  16. positive regulation of protein import into nucleus, translocation Source: Ensembl
  17. protein complex assembly Source: Ensembl
  18. protein localization to kinetochore Source: Ensembl
  19. protein phosphorylation Source: MGI
  20. response to activity Source: Ensembl
  21. response to amine Source: Ensembl
  22. response to axon injury Source: Ensembl
  23. response to cadmium ion Source: Ensembl
  24. response to copper ion Source: Ensembl
  25. response to drug Source: Ensembl
  26. response to ethanol Source: Ensembl
  27. response to organic cyclic compound Source: Ensembl
  28. response to toxic substance Source: Ensembl
  29. ventricular cardiac muscle cell development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 3474.
ReactomeiREACT_196577. MASTL Facilitates Mitotic Progression.
REACT_196580. Condensation of Prophase Chromosomes.
REACT_196632. Condensation of Prometaphase Chromosomes.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_196645. Activation of NIMA Kinases NEK9, NEK6, NEK7.
REACT_196650. Nuclear Pore Complex (NPC) Disassembly.
REACT_198608. G1/S-Specific Transcription.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199110. G0 and Early G1.
REACT_204224. Phosphorylation of Emi1.
REACT_204269. E2F-enabled inhibition of pre-replication complex formation.
REACT_205250. Phosphorylation of the APC/C.
REACT_206803. Cyclin A/B1 associated events during G2/M transition.
REACT_206830. E2F mediated regulation of DNA replication.
REACT_208718. Depolymerisation of the Nuclear Lamina.
REACT_209377. Cyclin B2 mediated events.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_223573. G2/M DNA replication checkpoint.
REACT_236786. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_243078. Loss of Nlp from mitotic centrosomes.
REACT_244487. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_245720. Recruitment of mitotic centrosome proteins and complexes.
REACT_246290. Recruitment of NuMA to mitotic centrosomes.
REACT_246476. Regulation of APC/C activators between G1/S and early anaphase.
REACT_247448. ERK1 activation.
REACT_257344. Golgi Cisternae Pericentriolar Stack Reorganization.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 1 (EC:2.7.11.22, EC:2.7.11.23)
Short name:
CDK1
Alternative name(s):
Cell division control protein 2 homolog
Cell division protein kinase 1
p34 protein kinase
Gene namesi
Name:Cdk1
Synonyms:Cdc2, Cdc2a, Cdkn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:88351. Cdk1.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication. Mitochondrion 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle By similarity
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.By similarity

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. extracellular vesicular exosome Source: Ensembl
  3. midbody Source: Ensembl
  4. mitochondrion Source: UniProtKB-KW
  5. mitotic spindle Source: UniProtKB
  6. nucleoplasm Source: Reactome
  7. nucleus Source: MGI
  8. spindle microtubule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality in the first cell divisions.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297Cyclin-dependent kinase 1PRO_0000085725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei4 – 41Phosphotyrosine; by PKRBy similarity
Modified residuei6 – 61N6-acetyllysine1 Publication
Modified residuei9 – 91N6-acetyllysine1 Publication
Modified residuei14 – 141Phosphothreonine; alternate1 Publication
Modified residuei14 – 141Phosphothreonine; by PKMYT1; alternateBy similarity
Modified residuei15 – 151Phosphotyrosine; by PKMYT1, WEE1, WEE2 and PKC/PRKCD; alternate4 Publications
Modified residuei15 – 151Phosphotyrosine; by WEE1 and WEE2; alternate4 Publications
Modified residuei19 – 191PhosphotyrosineBy similarity
Modified residuei39 – 391PhosphoserineBy similarity
Modified residuei77 – 771PhosphotyrosineBy similarity
Cross-linki89 – 89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei161 – 1611Phosphothreonine; by CAKBy similarity
Modified residuei178 – 1781PhosphoserineBy similarity
Modified residuei222 – 2221PhosphothreonineBy similarity
Modified residuei245 – 2451N6-succinyllysine1 Publication
Modified residuei248 – 2481PhosphoserineBy similarity

Post-translational modificationi

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.By similarity4 Publications
Polyubiquitinated upon genotoxic stress.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP11440.
PaxDbiP11440.
PRIDEiP11440.

PTM databases

PhosphoSiteiP11440.

Expressioni

Inductioni

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).Curated

Gene expression databases

BgeeiP11440.
CleanExiMM_CDC2A.
ExpressionAtlasiP11440. baseline and differential.
GenevestigatoriP11440.

Interactioni

Subunit structurei

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 (By similarity). Interacts with CEP63; this interaction recruits CDK1 to centrosomes (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Ccna2P519432EBI-846949,EBI-846980
Ccne1Q614572EBI-846949,EBI-643090
Pou5f1P202634EBI-846949,EBI-1606219

Protein-protein interaction databases

BioGridi198624. 104 interactions.
DIPiDIP-38725N.
IntActiP11440. 96 interactions.
MINTiMINT-4587254.

Structurei

3D structure databases

ProteinModelPortaliP11440.
SMRiP11440. Positions 1-289.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 287284Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119154.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP11440.
KOiK02087.
OMAiGKMALKH.
OrthoDBiEOG7966H8.
PhylomeDBiP11440.
TreeFamiTF101021.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11440-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEDYIKIEKI GEGTYGVVYK GRHRVTGQIV AMKKIRLESE EEGVPSTAIR
60 70 80 90 100
EISLLKELRH PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQFM
110 120 130 140 150
DSSLVKSYLH QILQGIVFCH SRRVLHRDLK PQNLLIDDKG TIKLADFGLA
160 170 180 190 200
RAFGIPIRVY THEVVTLWYR SPEVLLGSAR YSTPVDIWSI GTIFAELATK
210 220 230 240 250
KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNT FPKWKPGSLA
260 270 280 290
SHVKNLDENG LDLLSKMLVY DPAKRISGKM ALKHPYFDDL DNQIKKM
Length:297
Mass (Da):34,107
Last modified:August 1, 1991 - v3
Checksum:i9C399FCC41BA7F31
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121I → M in AAB09465. (PubMed:9895127)Curated
Sequence conflicti113 – 1131L → M AA sequence (PubMed:2662013)Curated
Sequence conflicti165 – 1651V → L in CAA34481. (PubMed:2132958)Curated
Sequence conflicti245 – 2451K → N AA sequence (PubMed:2662013)Curated
Sequence conflicti245 – 2451K → N in AAB09465. (PubMed:9895127)Curated
Sequence conflicti260 – 2601G → C AA sequence (PubMed:2662013)Curated
Sequence conflicti260 – 2601G → C in AAB09465. (PubMed:9895127)Curated
Sequence conflicti263 – 2631L → F AA sequence (PubMed:2662013)Curated
Sequence conflicti263 – 2631L → F in AAB09465. (PubMed:9895127)Curated
Sequence conflicti273 – 2731A → T in CAA34481. (PubMed:2132958)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38724 mRNA. Translation: AAA37408.1.
X16461 mRNA. Translation: CAA34481.1.
U58633 mRNA. Translation: AAB09465.1.
AK030231 mRNA. Translation: BAC26856.1.
AK135516 mRNA. Translation: BAE22561.1.
AK168054 mRNA. Translation: BAE40034.1.
BC024396 mRNA. Translation: AAH24396.1.
CCDSiCCDS23908.1.
PIRiA36074.
RefSeqiNP_031685.2. NM_007659.3.
UniGeneiMm.281367.

Genome annotation databases

EnsembliENSMUST00000020099; ENSMUSP00000020099; ENSMUSG00000019942.
ENSMUST00000119827; ENSMUSP00000113184; ENSMUSG00000019942.
GeneIDi12534.
KEGGimmu:12534.
UCSCiuc007fmr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38724 mRNA. Translation: AAA37408.1 .
X16461 mRNA. Translation: CAA34481.1 .
U58633 mRNA. Translation: AAB09465.1 .
AK030231 mRNA. Translation: BAC26856.1 .
AK135516 mRNA. Translation: BAE22561.1 .
AK168054 mRNA. Translation: BAE40034.1 .
BC024396 mRNA. Translation: AAH24396.1 .
CCDSi CCDS23908.1.
PIRi A36074.
RefSeqi NP_031685.2. NM_007659.3.
UniGenei Mm.281367.

3D structure databases

ProteinModelPortali P11440.
SMRi P11440. Positions 1-289.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198624. 104 interactions.
DIPi DIP-38725N.
IntActi P11440. 96 interactions.
MINTi MINT-4587254.

Chemistry

BindingDBi P11440.
ChEMBLi CHEMBL4084.

PTM databases

PhosphoSitei P11440.

Proteomic databases

MaxQBi P11440.
PaxDbi P11440.
PRIDEi P11440.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020099 ; ENSMUSP00000020099 ; ENSMUSG00000019942 .
ENSMUST00000119827 ; ENSMUSP00000113184 ; ENSMUSG00000019942 .
GeneIDi 12534.
KEGGi mmu:12534.
UCSCi uc007fmr.1. mouse.

Organism-specific databases

CTDi 983.
MGIi MGI:88351. Cdk1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119154.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi P11440.
KOi K02087.
OMAi GKMALKH.
OrthoDBi EOG7966H8.
PhylomeDBi P11440.
TreeFami TF101021.

Enzyme and pathway databases

BRENDAi 2.7.11.22. 3474.
Reactomei REACT_196577. MASTL Facilitates Mitotic Progression.
REACT_196580. Condensation of Prophase Chromosomes.
REACT_196632. Condensation of Prometaphase Chromosomes.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_196645. Activation of NIMA Kinases NEK9, NEK6, NEK7.
REACT_196650. Nuclear Pore Complex (NPC) Disassembly.
REACT_198608. G1/S-Specific Transcription.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199110. G0 and Early G1.
REACT_204224. Phosphorylation of Emi1.
REACT_204269. E2F-enabled inhibition of pre-replication complex formation.
REACT_205250. Phosphorylation of the APC/C.
REACT_206803. Cyclin A/B1 associated events during G2/M transition.
REACT_206830. E2F mediated regulation of DNA replication.
REACT_208718. Depolymerisation of the Nuclear Lamina.
REACT_209377. Cyclin B2 mediated events.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_223573. G2/M DNA replication checkpoint.
REACT_236786. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_243078. Loss of Nlp from mitotic centrosomes.
REACT_244487. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_245720. Recruitment of mitotic centrosome proteins and complexes.
REACT_246290. Recruitment of NuMA to mitotic centrosomes.
REACT_246476. Regulation of APC/C activators between G1/S and early anaphase.
REACT_247448. ERK1 activation.
REACT_257344. Golgi Cisternae Pericentriolar Stack Reorganization.

Miscellaneous databases

NextBioi 281570.
PROi P11440.
SOURCEi Search...

Gene expression databases

Bgeei P11440.
CleanExi MM_CDC2A.
ExpressionAtlasi P11440. baseline and differential.
Genevestigatori P11440.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The FT210 cell line is a mouse G2 phase mutant with a temperature-sensitive CDC2 gene product."
    Th'Ng J.P.H., Wright P.S., Hamaguchi J., Lee M.G., Norbury C.J., Nurse P., Bradbury E.M.
    Cell 63:313-324(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FM3A.
    Tissue: Mammary carcinoma.
  2. "Cloning of the mouse homologue of the yeast cell cycle control gene cdc2."
    Spurr N.K., Gough A.C., Lee M.G.
    DNA Seq. 1:49-54(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  3. "Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2."
    Cisek L.J., Corden J.L.
    Nature 339:679-684(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  4. "Characterization of the murine cdc2 gene."
    Jun D., Park H.K., Nordin A.A., Nagel J.E., Kim Y.H.
    Mol. Cells 8:731-740(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  5. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Muellerian duct and Testis.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.
  7. "Wee1B is an oocyte-specific kinase involved in the control of meiotic arrest in the mouse."
    Han S.J., Chen R., Paronetto M.P., Conti M.
    Curr. Biol. 15:1670-1676(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-15.
  8. "Cdc2-cyclin E complexes regulate the G1/S phase transition."
    Aleem E., Kiyokawa H., Kaldis P.
    Nat. Cell Biol. 7:831-836(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AT THE TRANSITION G1-S, INTERACTION WITH CDKN1B/P27 AND CYCLIN E1, REGULATION BY CDKN1B/P27.
  9. Cited for: FUNCTION IN CELL CYCLE REGULATION, DISRUPTION PHENOTYPE.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "p21 Inhibits Cdk1 in the absence of Cdk2 to maintain the G1/S phase DNA damage checkpoint."
    Satyanarayana A., Hilton M.B., Kaldis P.
    Mol. Biol. Cell 19:65-77(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDKN1A/P21, SUBCELLULAR LOCATION, ENZYME REGULATION BY CDKN1A/P21.
  12. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  13. "The protein kinase Cdelta catalytic fragment is critical for maintenance of the G2/M DNA damage checkpoint."
    LaGory E.L., Sitailo L.A., Denning M.F.
    J. Biol. Chem. 285:1879-1887(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-15.
  14. "Protein tyrosine kinase Wee1B is essential for metaphase II exit in mouse oocytes."
    Oh J.S., Susor A., Conti M.
    Science 332:462-465(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-15.
  15. "Tex14, a plk1-regulated protein, is required for kinetochore-microtubule attachment and regulation of the spindle assembly checkpoint."
    Mondal G., Ohashi A., Yang L., Rowley M., Couch F.J.
    Mol. Cell 45:680-695(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TEX14.
  16. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    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.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-6 AND LYS-9, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCDK1_MOUSE
AccessioniPrimary (citable) accession number: P11440
Secondary accession number(s): P70337, Q3TI12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 1, 1991
Last modified: November 26, 2014
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3