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P06493 (CDK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 186. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase 1

Short name=CDK1
EC=2.7.11.22
EC=2.7.11.23
Alternative name(s):
Cell division control protein 2 homolog
Cell division protein kinase 1
p34 protein kinase
Gene names
Name:CDK1
Synonyms:CDC2, CDC28A, CDKN1, P34CDC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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, 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 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. Ref.15 Ref.16 Ref.18 Ref.20 Ref.24 Ref.25 Ref.29 Ref.30 Ref.32 Ref.33 Ref.34 Ref.35 Ref.39

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

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

Enzyme regulation

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-161 activates it. Activated through a multistep process; binding to cyclin-B is required for relocation of cyclin-kinase complexes to the nucleus, activated by CAK/CDK7-mediated phosphorylation on Thr-161, and CDC25-mediated dephosphorylation of inhibitory phosphorylation on Thr-14 and Tyr-15. Inhibited by flavopiridol and derivatives, pyrimidine derivatives, pyridine derivatives, purine derivatives, staurosporine, paullones, oxoindoles, indazole analogs, indolin-2-ones, pyrazolo[3,4-b]pyridines, imidazo[1,2-a]pyridine (AZ703), thiazolinone analogs(RO-3306), thiazol urea, macrocyclic quinoxalin-2-one, pyrrolo[2,3-a]carbazole, pyrazolo[1,5-a]-1,3,5-triazine, pyrazolo[1,5-a]pyrimidine (Dinaciclib, SCH 727965), 2-(1-ethyl-2-hydroxyethylamino)-6-benzylamino-9-isopropylpurine (roscovitine), olomoucine, AG-024322, AT-7519, P276-00, R547/Ro-4584820 and SNS-032/BMS-387032. 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. Ref.12 Ref.18

Subunit structure

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. Ref.11 Ref.13 Ref.14 Ref.24 Ref.32 Ref.38

Subcellular location

Nucleus. Cytoplasm. Mitochondrion. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: 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. Ref.33 Ref.38

Tissue specificity

Isoform 2 is found in breast cancer tissues.

Induction

Follows 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, but later repressed. Triggered by CKS1B during mitotic entry in breast cancer cells. Down-regulated under genotoxic stresses triggered by PKR/EIF2AK2-mediated phosphorylation. Ref.12 Ref.17 Ref.18

Post-translational modification

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. In response to UV irradiation, phosphorylation at Tyr-15 by PRKCD activates the G2/M DNA damage checkpoint. Ref.9 Ref.10 Ref.30 Ref.31 Ref.32

Polyubiquitinated upon genotoxic stress.

Miscellaneous

As a key regulator of the cell cycle, CDK1 is a potent therapeutic target for inhibitors in cancer treatment (Ref.44).

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence EAW54204.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement Ref.45. Source: UniProtKB

DNA replication

Traceable author statement Ref.45. Source: UniProtKB

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

Ras protein signal transduction

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement. Source: Reactome

activation of MAPKK activity

Traceable author statement. Source: Reactome

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

axon guidance

Traceable author statement. Source: Reactome

cell aging

Inferred from electronic annotation. Source: Ensembl

cell migration

Traceable author statement PubMed 17200138. Source: UniProtKB

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

centrosome cycle

Traceable author statement Ref.41. Source: UniProtKB

chromosome condensation

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

epithelial cell differentiation

Inferred from expression pattern PubMed 21492153. Source: UniProt

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic G2 DNA damage checkpoint

Inferred from electronic annotation. Source: Ensembl

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from direct assay PubMed 11069302. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

organ regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of cardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein import into nucleus, translocation

Inferred from electronic annotation. Source: Ensembl

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

pronuclear fusion

Traceable author statement Ref.43. Source: UniProtKB

protein complex assembly

Inferred from electronic annotation. Source: Ensembl

protein localization to kinetochore

Inferred from direct assay PubMed 18195732. Source: BHF-UCL

regulation of Schwann cell differentiation

Traceable author statement PubMed 17200138. Source: UniProtKB

regulation of embryonic development

Traceable author statement Ref.43. Source: UniProtKB

regulation of transcription involved in G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

response to activity

Inferred from electronic annotation. Source: Ensembl

response to amine

Inferred from electronic annotation. Source: Ensembl

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to copper ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

ventricular cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from direct assay PubMed 11069302. Source: UniProtKB

mitochondrion

Traceable author statement Ref.33. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

spindle microtubule

Inferred from direct assay PubMed 11069302. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from direct assay PubMed 12721286. Source: UniProtKB

cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay PubMed 11069302PubMed 18477460. Source: UniProtKB

histone kinase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06493-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P06493-2)

Also known as: CDC2deltaT;

The sequence of this isoform differs from the canonical sequence as follows:
     107-163: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Cyclin-dependent kinase 1
PRO_0000085724

Regions

Domain4 – 287284Protein kinase
Nucleotide binding10 – 189ATP By similarity

Sites

Active site1281Proton acceptor By similarity
Binding site331ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.26 Ref.28 Ref.47
Modified residue41Phosphotyrosine; by PKR Ref.30
Modified residue61N6-acetyllysine Ref.28
Modified residue91N6-acetyllysine By similarity
Modified residue141Phosphothreonine; by PKMYT1 Ref.10 Ref.22 Ref.27 Ref.32
Modified residue151Phosphotyrosine; by PKMYT1, WEE1, WEE2 and PKC/PRKCD Ref.10 Ref.22 Ref.27 Ref.31 Ref.32
Modified residue191Phosphotyrosine Ref.21 Ref.26
Modified residue391Phosphoserine Ref.21 Ref.26
Modified residue771Phosphotyrosine Ref.21
Modified residue1611Phosphothreonine; by CAK Ref.27 Ref.32 Ref.36 Ref.46
Modified residue1781Phosphoserine Ref.26
Modified residue2221Phosphothreonine Ref.21 Ref.26
Modified residue2451N6-succinyllysine By similarity
Modified residue2481Phosphoserine Ref.26
Cross-link89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.23

Natural variations

Alternative sequence107 – 16357Missing in isoform 2.
VSP_021375

Experimental info

Mutagenesis41Y → D or E: Constitutive polyubiquitination. Ref.20 Ref.30
Mutagenesis14 – 152TY → AF: Abnormal cell cycle exhibiting only M-phase without completing either karyokinesis or cytokinesis. Ref.20

Secondary structure

................................................. 297
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 31, 2011. Version 3.
Checksum: 942D79448EFE490A

FASTA29734,095
        10         20         30         40         50         60 
MEDYTKIEKI GEGTYGVVYK GRHKTTGQVV AMKKIRLESE EEGVPSTAIR EISLLKELRH 

        70         80         90        100        110        120 
PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQYM DSSLVKSYLY QILQGIVFCH 

       130        140        150        160        170        180 
SRRVLHRDLK PQNLLIDDKG TIKLADFGLA RAFGIPIRVY THEVVTLWYR SPEVLLGSAR 

       190        200        210        220        230        240 
YSTPVDIWSI GTIFAELATK KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNT 

       250        260        270        280        290 
FPKWKPGSLA SHVKNLDENG LDLLSKMLIY DPAKRISGKM ALNHPYFNDL DNQIKKM 

« Hide

Isoform 2 (CDC2deltaT) [UniParc].

Checksum: 50FC3D192024E38C
Show »

FASTA24027,503

References

« Hide 'large scale' references
[1]"Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2."
Lee M.G., Nurse P.
Nature 327:31-35(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"T-loop deletion of CDC2 from breast cancer tissues eliminates binding to cyclin B1 and cyclin-dependent kinase inhibitor p21."
Ohta T., Okamoto K., Isohashi F., Shibata K., Fukuda M., Yamaguchi S., Xiong Y.
Cancer Res. 58:1095-1098(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Mammary cancer.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]NIEHS SNPs program
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 1).
Tissue: Skin.
[9]"Activation of cdc2 protein kinase during mitosis in human cells: cell cycle-dependent phosphorylation and subunit rearrangement."
Draetta G., Beach D.
Cell 54:17-26(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, ASSOCIATION WITH P13.
[10]"Myt1: a membrane-associated inhibitory kinase that phosphorylates Cdc2 on both threonine-14 and tyrosine-15."
Mueller P.R., Coleman T.R., Kumagai A., Dunphy W.G.
Science 270:86-90(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-14 AND TYR-15 BY PKMYT1.
[11]"The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase, cdc2."
Kupfer G.M., Yamashita T., Naf D., Suliman A., Asano S., D'Andrea A.D.
Blood 90:1047-1054(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FANCC.
[12]"Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5."
Meijer L., Borgne A., Mulner O., Chong J.P.J., Blow J.J., Inagaki N., Inagaki M., Delcros J.-G., Moulinoux J.-P.
Eur. J. Biochem. 243:527-536(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION BY ROSCOVITINE AND OLOMOUCINE.
[13]"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis."
Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.
J. Biol. Chem. 278:30597-30604(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RALBP1.
[14]"Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region."
Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.
J. Biol. Chem. 279:32592-32602(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLGAP5.
[15]"Cell cycle-dependent phosphorylation of the RUNX2 transcription factor by cdc2 regulates endothelial cell proliferation."
Qiao M., Shapiro P., Fosbrink M., Rus H., Kumar R., Passaniti A.
J. Biol. Chem. 281:7118-7128(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS RUNX2 KINASE.
[16]"Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-dependent kinase Cdk1."
Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I., Juillan-Binard C., Lantez V., Job D.
Mol. Biol. Cell 17:1041-1050(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS BETA-TUBULINS KINASE.
[17]"Cks1 regulates cdk1 expression: a novel role during mitotic entry in breast cancer cells."
Westbrook L., Manuvakhova M., Kern F.G., Estes N.R. II, Ramanathan H.N., Thottassery J.V.
Cancer Res. 67:11393-11401(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY CKS1B.
[18]"TGFbeta regulates the expression and activities of G2 checkpoint kinases in human myeloid leukemia cells."
Hu X., Cui D., Moscinski L.C., Zhang X., Maccachero V., Zuckerman K.S.
Cytokine 37:155-162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS RB1 KINASE, ENZYME REGULATION BY TGFB1, REPRESSION BY TGFB1.
[19]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Rapid cycling and precocious termination of G1 phase in cells expressing CDK1AF."
Pomerening J.R., Ubersax J.A., Ferrell J.E. Jr.
Mol. Biol. Cell 19:3426-3441(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION DURING THE M PHASE, MUTAGENESIS OF 14-THR-TYR-15.
[21]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19; SER-39; TYR-77 AND THR-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells."
Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.
Proteomics 8:2885-2896(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-89.
Tissue: Cervix carcinoma.
[24]"Activation of FOXO1 by Cdk1 in cycling cells and postmitotic neurons."
Yuan Z., Becker E.B.E., Merlo P., Yamada T., DiBacco S., Konishi Y., Schaefer E.M., Bonni A.
Science 319:1665-1668(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS FOXO1 KINASE, INTERACTION WITH FOXO1.
[25]"Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for targeting of the gammaTuRC to the centrosome."
Zhang X., Chen Q., Feng J., Hou J., Yang F., Liu J., Jiang Q., Zhang C.
J. Cell Sci. 122:2240-2251(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS NEDD1 KINASE.
[26]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19; SER-39; SER-178; THR-222 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15 AND THR-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[28]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND LYS-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Mitotic phosphorylation of Aki1 at Ser208 by cyclin B1-Cdk1 complex."
Nakamura A., Naito M., Arai H., Fujita N.
Biochem. Biophys. Res. Commun. 393:872-876(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CC2D1A KINASE.
[30]"New Cdc2 Tyr 4 phosphorylation by dsRNA-activated protein kinase triggers Cdc2 polyubiquitination and G2 arrest under genotoxic stresses."
Yoon C.-H., Miah M.A., Kim K.P., Bae Y.-S.
EMBO Rep. 11:393-399(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN G2 ARREST UPON DNA DAMAGE, PHOSPHORYLATION AT TYR-4 BY PKR/EIF2AK2, POLYUBIQUITINATION, MUTAGENESIS OF TYR-4.
[31]"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.
[32]"Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B at the G2/M transition."
Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.
J. Biol. Chem. 285:16978-16990(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN G2-M TRANSITION, DEPHOSPHORYLATION AT THR-14 AND TYR-15 BY CDC25, PHOSPHORYLATION AT THR-161 BY CDK7/CAK, INTERACTION WITH B-CYCLIN.
[33]"Cyclin-dependent kinase 1-mediated Bcl-xL/Bcl-2 phosphorylation acts as a functional link coupling mitotic arrest and apoptosis."
Terrano D.T., Upreti M., Chambers T.C.
Mol. Cell. Biol. 30:640-656(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS BCL-XL/BCL2L1 KINASE, SUBCELLULAR LOCATION.
[34]"Cdk1/cyclin B1 controls Fas-mediated apoptosis by regulating caspase-8 activity."
Matthess Y., Raab M., Sanhaji M., Lavrik I.N., Strebhardt K.
Mol. Cell. Biol. 30:5726-5740(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CASP8 KINASE.
[35]"Cyclin-dependent kinases regulate epigenetic gene silencing through phosphorylation of EZH2."
Chen S., Bohrer L.R., Rai A.N., Pan Y., Gan L., Zhou X., Bagchi A., Simon J.A., Huang H.
Nat. Cell Biol. 12:1108-1114(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS EZH2 KINASE.
[36]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[37]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"Cep63 recruits Cdk1 to the centrosome: implications for regulation of mitotic entry, centrosome amplification, and genome maintenance."
Loffler H., Fechter A., Matuszewska M., Saffrich R., Mistrik M., Marhold J., Hornung C., Westermann F., Bartek J., Kramer A.
Cancer Res. 71:2129-2139(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CEP63, SUBCELLULAR LOCATION.
[39]"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CHAMP1 KINASE.
[40]"Mammalian cyclin-dependent kinases."
Malumbres M., Barbacid M.
Trends Biochem. Sci. 30:630-641(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON SUBSTRATES, GENE FAMILY.
[41]"The decision to enter mitosis: feedback and redundancy in the mitotic entry network."
Lindqvist A., Rodriguez-Bravo V., Medema R.H.
J. Cell Biol. 185:193-202(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON SUBCELLULAR TRANSLOCATION.
[42]"Cell cycle, CDKs and cancer: a changing paradigm."
Malumbres M., Barbacid M.
Nat. Rev. Cancer 9:153-166(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON CELL CYCLE CONTROL AND INHIBITORS, GENE FAMILY.
[43]"Cdc2: a monopotent or pluripotent CDK?"
Hu X., Moscinski L.C.
Cell Prolif. 44:205-211(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON CELL CYCLE CONTROL.
[44]"Cyclin dependent kinase 1 inhibitors: a review of recent progress."
Wang Q., Su L., Liu N., Zhang L., Xu W., Fang H.
Curr. Med. Chem. 18:2025-2043(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON CELL CYCLE CONTROL AND INHIBITORS.
[45]"Checkpoint recovery in cells: how a molecular understanding can help in the fight against cancer."
Medema R.H., Macurek L.
F1000 Biol. Rep. 3:10-10(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON CELL CYCLE CONTROL.
[46]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[47]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05360 mRNA. Translation: CAA28963.1.
Y00272 mRNA. Translation: CAA68376.1.
D88357 mRNA. Translation: BAA26001.1.
AK291939 mRNA. Translation: BAF84628.1.
BT007004 mRNA. Translation: AAP35650.1.
AF512554 Genomic DNA. Translation: AAM34793.1.
AC022390 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54204.1. Sequence problems.
BC014563 mRNA. Translation: AAH14563.1.
PIRA29539.
RefSeqNP_001777.1. NM_001786.4.
NP_203698.1. NM_033379.4.
XP_005270360.1. XM_005270303.1.
UniGeneHs.732435.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LC9model-A1-297[»]
ProteinModelPortalP06493.
SMRP06493. Positions 1-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107420. 153 interactions.
DIPDIP-35N.
IntActP06493. 66 interactions.
MINTMINT-5000894.
STRING9606.ENSP00000306043.

Chemistry

BindingDBP06493.
ChEMBLCHEMBL1907602.
GuidetoPHARMACOLOGY1961.

PTM databases

PhosphoSiteP06493.

Polymorphism databases

DMDM288558822.

2D gel databases

SWISS-2DPAGEP06493.

Proteomic databases

PaxDbP06493.
PRIDEP06493.

Protocols and materials databases

DNASU983.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316629; ENSP00000325970; ENSG00000170312. [P06493-2]
ENST00000373809; ENSP00000362915; ENSG00000170312. [P06493-2]
ENST00000395284; ENSP00000378699; ENSG00000170312. [P06493-1]
GeneID983.
KEGGhsa:983.
UCSCuc001jld.3. human. [P06493-1]
uc001jlg.3. human. [P06493-2]

Organism-specific databases

CTD983.
GeneCardsGC10P062539.
HGNCHGNC:1722. CDK1.
HPACAB003799.
HPA003387.
MIM116940. gene.
neXtProtNX_P06493.
PharmGKBPA99.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG014652.
KOK02087.
OMAPNNDVWP.
TreeFamTF101021.

Enzyme and pathway databases

BRENDA2.7.11.22. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
SignaLinkP06493.

Gene expression databases

ArrayExpressP06493.
BgeeP06493.
CleanExHS_CDC2.
GenevestigatorP06493.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDK1. human.
GeneWikiCdk1.
Cyclin-dependent_kinase_1.
GenomeRNAi983.
NextBio4122.
PROP06493.
SOURCESearch...

Entry information

Entry nameCDK1_HUMAN
AccessionPrimary (citable) accession number: P06493
Secondary accession number(s): A8K7C4, C9J497, O60764
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: May 31, 2011
Last modified: March 19, 2014
This is version 186 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM