P06493 (CDK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Protein existence	Evidence 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.16 Ref.17 Ref.19 Ref.21 Ref.25 Ref.26 Ref.30 Ref.31 Ref.33 Ref.34 Ref.35 Ref.36 Ref.40
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.19
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.25 Ref.33 Ref.39
Subcellular location	Nucleus. Cytoplasm. Mitochondrion. Cytoplasm › cytoskeleton › centrosome. 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.34 Ref.39
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.18 Ref.19
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.31 Ref.32 Ref.33 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.45).
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 process	Apoptosis Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Traceable author statement Ref.46. Source: UniProtKB DNA replication Traceable author statement Ref.46. Source: UniProtKB 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 Toll 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: Compara cell cycle checkpoint Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW cell migration Traceable author statement PubMed 17200138. Source: UniProtKB cellular response to hydrogen peroxide Inferred from electronic annotation. Source: Compara centrosome cycle Traceable author statement Ref.42. Source: UniProtKB chromosome condensation Inferred from electronic annotation. Source: Compara epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome 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: Compara negative regulation of apoptotic process Inferred from direct assay PubMed 11069302. Source: UniProtKB nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome organ regeneration Inferred from electronic annotation. Source: Compara positive regulation of DNA replication Inferred from electronic annotation. Source: Compara positive regulation of cardiac muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of gene expression Inferred from electronic annotation. Source: Compara positive regulation of mitotic cell cycle Inferred from electronic annotation. Source: Compara positive regulation of protein import into nucleus, translocation Inferred from electronic annotation. Source: Compara positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome pronuclear fusion Traceable author statement Ref.44. Source: UniProtKB protein complex assembly Inferred from electronic annotation. Source: Compara 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.44. Source: UniProtKB regulation of transcription involved in G1/S phase of mitotic cell cycle Traceable author statement. Source: Reactome response to activity Inferred from electronic annotation. Source: Compara response to amine stimulus Inferred from electronic annotation. Source: Compara response to axon injury Inferred from electronic annotation. Source: Compara response to cadmium ion Inferred from electronic annotation. Source: Compara response to copper ion Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from electronic annotation. Source: Compara response to toxin Inferred from electronic annotation. Source: Compara stress-activated MAPK cascade Traceable author statement. Source: Reactome toll-like receptor 1 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 ventricular cardiac muscle cell development Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from direct assay PubMed 11069302. Source: UniProtKB mitochondrion Traceable author statement Ref.34. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome spindle microtubule Inferred from direct assay PubMed 11069302. Source: UniProtKB
Molecular_function	ATP 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: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BIRC5	O15392	6	EBI-444308,EBI-518823
CCNB1	P14635	4	EBI-444308,EBI-495332
CDC25C	P30307	2	EBI-444308,EBI-974439
FOXO1	Q12778	5	EBI-444308,EBI-1108782
LATS1	O95835	2	EBI-444308,EBI-444209
PKMYT1	Q99640	2	EBI-444308,EBI-495308

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 297

297

Cyclin-dependent kinase 1

PRO_0000085724

Regions

Domain

4 – 287

284

Protein kinase

Nucleotide binding

10 – 18

9

ATP By similarity

Sites

Active site

128

1

Proton acceptor By similarity

Binding site

33

1

ATP By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.27 Ref.29

Modified residue

4

1

Phosphotyrosine; by PKR Ref.31

Modified residue

6

1

N6-acetyllysine Ref.29

Modified residue

14

1

Phosphothreonine; by PKMYT1 Ref.10 Ref.23 Ref.28 Ref.33

Modified residue

15

1

Phosphotyrosine; by PKMYT1, WEE1, WEE2 and PKC/PRKCD Ref.10 Ref.23 Ref.28 Ref.32 Ref.33

Modified residue

19

1

Phosphotyrosine Ref.22 Ref.27

Modified residue

39

1

Phosphoserine Ref.22 Ref.27

Modified residue

77

1

Phosphotyrosine Ref.22

Modified residue

161

1

Phosphothreonine; by CAK Ref.28 Ref.33 Ref.37 Ref.47

Modified residue

178

1

Phosphoserine Ref.27

Modified residue

222

1

Phosphothreonine Ref.22 Ref.27

Modified residue

248

1

Phosphoserine Ref.27

Cross-link

89

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.24

Natural variations

Alternative sequence

107 – 163

57

Missing in isoform 2.

VSP_021375

Experimental info

Mutagenesis

4

1

Y → D or E: Constitutive polyubiquitination. Ref.21 Ref.31

Mutagenesis

14 – 15

2

TY → AF: Abnormal cell cycle exhibiting only M-phase without completing either karyokinesis or cytokinesis. Ref.21

Secondary structure

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297

Helix Strand Turn

Details...

Beta strand

4 – 12

9

Beta strand

14 – 23

10

Turn

24 – 26

3

Beta strand

29 – 36

8

Beta strand

39 – 42

4

Helix

46 – 57

12

Beta strand

66 – 71

6

Beta strand

73 – 81

9

Beta strand

84 – 86

3

Helix

87 – 93

7

Beta strand

94 – 96

3

Helix

102 – 121

20

Beta strand

133 – 136

4

Beta strand

142 – 144

3

Helix

167 – 169

3

Helix

172 – 176

5

Helix

184 – 199

16

Helix

209 – 220

12

Turn

225 – 227

3

Beta strand

234 – 236

3

Helix

249 – 252

4

Turn

253 – 255

3

Helix

258 – 267

10

Turn

272 – 274

3

Helix

278 – 283

6

Helix

285 – 287

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 31, 2011. Version 3. Checksum: 942D79448EFE490A	FASTA	297	34,095
	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
	Isoform 2 (CDC2deltaT) [UniParc]. Checksum: 50FC3D192024E38C	FASTA	240	27,503
	10 20 30 40 50 60 MEDYTKIEKI GEGTYGVVYK GRHKTTGQVV AMKKIRLESE EEGVPSTAIR EISLLKELRH 70 80 90 100 110 120 PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQYM DSSLVKVVTL WYRSPEVLLG 130 140 150 160 170 180 SARYSTPVDI WSIGTIFAEL ATKKPLFHGD SEIDQLFRIF RALGTPNNEV WPEVESLQDY 190 200 210 220 230 240 KNTFPKWKPG SLASHVKNLD ENGLDLLSKM LIYDPAKRIS GKMALNHPYF NDLDNQIKKM

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"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.
[26]	"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.
[27]	"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, MASS SPECTROMETRY.
[28]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[29]	"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, MASS SPECTROMETRY.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[38]	"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].
[39]	"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.
[40]	"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.
[41]	"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.
[42]	"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.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.

IPI

IPI00026689.
IPI00073536.

PIR

A29539.

RefSeq

NP_001777.1. NM_001786.4.
NP_203698.1. NM_033379.4.

UniGene

Hs.732435.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LC9	model	-	A	1-297	[»]

ProteinModelPortal

P06493.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35N.

IntAct

P06493. 45 interactions.

MINT

MINT-5000894.

STRING

9606.ENSP00000306043.

PTM databases

PhosphoSite

P06493.

Polymorphism databases

DMDM

288558822.

2D gel databases

SWISS-2DPAGE

P06493.

Proteomic databases

PaxDb

P06493.

PRIDE

P06493.

Protocols and materials databases

DNASU

983.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000316629; ENSP00000325970; ENSG00000170312.
ENST00000373809; ENSP00000362915; ENSG00000170312.
ENST00000395284; ENSP00000378699; ENSG00000170312.
ENST00000448257; ENSP00000397973; ENSG00000170312.

GeneID

983.

KEGG

hsa:983.

UCSC

uc001jld.3. human.
uc001jlg.3. human.

Organism-specific databases

CTD

983.

GeneCards

GC10P062539.

HGNC

HGNC:1722. CDK1.

HPA

CAB003799.
HPA003387.

MIM

116940. gene.

neXtProt

NX_P06493.

PharmGKB

PA99.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG014652.

KO

K02087.

OMA

PNNDVWP.

OrthoDB

EOG41NTMH.

Enzyme and pathway databases

BRENDA

2.7.11.22. 2681.

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.

Reactome

REACT_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.

Gene expression databases

ArrayExpress

P06493.

Bgee

P06493.

CleanEx

HS_CDC2.

Genevestigator

P06493.

GermOnline

ENSG00000170312. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P06493.

ChEMBL

CHEMBL308.

ChiTaRS

CDK1. human.

GenomeRNAi

983.

NextBio

4122.

SOURCE

Search...

Entry information

Entry name

CDK1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 176 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.