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P24941 (CDK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 185. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 2

EC=2.7.11.22
Alternative name(s):
Cell division protein kinase 2
p33 protein kinase
Gene names
Name:CDK2
Synonyms:CDKN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 By similarity. Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.26 Ref.29 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.42 Ref.44 Ref.45 Ref.63

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-160 activates it. Inhibited by 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3), AG-024322, N-(4-Piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H-pyrazole-3-carboxamide (AT7519), R547 (Ro-4584820), purine, pyrimidine and pyridine derivatives, 2-aminopyrimidines, paullones, thiazo derivatives, macrocyclic quinoxalin-2-one, pyrazolo[1,5-a]-1,3,5-triazine, pyrazolo[1,5-a]pyrimidine, 2-(1-ethyl-2-hydroxyethylamino)-6-benzylamino-9-isopropylpurine (roscovitine, seliciclib and CYC202), SNS-032 (BMS-387032), triazolo[1,5-a]pyrimidines, staurosporine and olomoucine. Stimulated by MYC. Inactivated by CDKN1A (p21). Ref.12 Ref.34 Ref.59

Subunit structure

Found in a complex with CABLES1, CCNA1 and CCNE1. Interacts with CABLES1 By similarity. Interacts with UHRF2. Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts with the Speedy/Ringo proteins SPDYA and SPDYC. Found in a complex with both SPDYA and CDKN1B/KIP1. Binds to RB1 and CDK7. Binding to CDKN1A (p21) leads to CDK2/cyclin E inactivation at the G1-S phase DNA damage checkpoint, thereby arresting cells at the G1-S transition during DNA repair. Associated with PTPN6 and beta-catenin/CTNNB1. Interacts with CACUL1. May interact with CEP63. Ref.13 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.27 Ref.30 Ref.41 Ref.42 Ref.46

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. NucleusCajal body. Cytoplasm. Endosome. Note: Localized at the centrosomes in late G2 phase after separation of the centrosomes but before the start of prophase. Nuclear-cytoplasmic trafficking is mediated during the inhibition by 1,25-(OH)2D3. Ref.16 Ref.29 Ref.34 Ref.42

Induction

Induced transiently by TGFB1 at an early phase of TGFB1-mediated apoptosis. Ref.12 Ref.34 Ref.59

Post-translational modification

Phosphorylated at Thr-160 by CDK7 in a CAK complex. Phosphorylation at Thr-160 promotes kinase activity, whereas phosphorylation at Tyr-15 by WEE1 reduces slightly kinase activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2 phases before being dephosphorylated by CDC25A. Ref.11 Ref.18 Ref.24 Ref.27 Ref.34 Ref.36 Ref.61 Ref.62 Ref.64 Ref.67

Nitrosylated after treatment with nitric oxide (DETA-NO).

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA repair
Meiosis
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Endosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Traceable author statement. Source: Reactome

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

DNA replication

Traceable author statement Ref.47. Source: UniProtKB

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Non-traceable author statement Ref.2. Source: UniProtKB

Ras protein signal transduction

Inferred from expression pattern PubMed 9054499. Source: BHF-UCL

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

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cellular response to nitric oxide

Traceable author statement Ref.35. Source: UniProtKB

centrosome duplication

Traceable author statement Ref.47. Source: UniProtKB

histone phosphorylation

Inferred from direct assay PubMed 8692841. Source: GOC

meiotic nuclear division

Traceable author statement Ref.47. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic G1 DNA damage checkpoint

Traceable author statement Ref.45. Source: UniProtKB

mitotic G2 phase

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of DNA-dependent DNA replication initiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from direct assay PubMed 10767298. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

potassium ion transport

Inferred from electronic annotation. Source: Ensembl

regulation of gene silencing

Inferred from direct assay Ref.37. Source: UniProtKB

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

Traceable author statement. Source: Reactome

   Cellular_componentCajal body

Inferred from direct assay Ref.16. Source: UniProtKB

X chromosome

Inferred from electronic annotation. Source: Ensembl

Y chromosome

Inferred from electronic annotation. Source: Ensembl

centrosome

Traceable author statement Ref.47. Source: UniProtKB

chromosome, telomeric region

Inferred from electronic annotation. Source: Ensembl

condensed chromosome

Inferred from electronic annotation. Source: Ensembl

cyclin-dependent protein kinase holoenzyme complex

Inferred from direct assay PubMed 8692841. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 10767298. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endosome

Inferred from direct assay Ref.42. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10767298. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclin binding

Inferred from direct assay Ref.2. Source: UniProtKB

cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay Ref.44. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P24941-1)

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: P24941-2)

Also known as: CDK2deltaT;

The sequence of this isoform differs from the canonical sequence as follows:
     163-196: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Cyclin-dependent kinase 2
PRO_0000085769

Regions

Domain4 – 286283Protein kinase
Nucleotide binding10 – 189ATP
Nucleotide binding81 – 833ATP
Nucleotide binding129 – 1324ATP

Sites

Active site1271Proton acceptor
Metal binding1321Magnesium; catalytic
Metal binding1451Magnesium; catalytic
Binding site331ATP
Binding site861ATP
Binding site1451ATP
Site91CDK7 binding
Site88 – 892CDK7 binding
Site1661CDK7 binding

Amino acid modifications

Modified residue11N-acetylmethionine Ref.33 Ref.51
Modified residue61N6-acetyllysine Ref.33
Modified residue141Phosphothreonine Ref.11 Ref.64
Modified residue151Phosphotyrosine; by WEE1 Ref.11 Ref.32 Ref.64
Modified residue191Phosphotyrosine Ref.31
Modified residue1601Phosphothreonine; by CAK and CCRK Ref.11 Ref.24 Ref.34 Ref.36 Ref.61 Ref.62 Ref.64 Ref.67

Natural variations

Alternative sequence163 – 19634Missing in isoform 2.
VSP_041998
Natural variant151Y → S.
Corresponds to variant rs3087335 [ dbSNP | Ensembl ].
VAR_016157
Natural variant181V → L.
Corresponds to variant rs11554376 [ dbSNP | Ensembl ].
VAR_053927
Natural variant451P → L in a glioblastoma multiforme sample; somatic mutation. Ref.68
VAR_041972
Natural variant2901T → S. Ref.6 Ref.68
Corresponds to variant rs2069413 [ dbSNP | Ensembl ].
VAR_019988

Experimental info

Mutagenesis91K → F: Reduced phosphorylation by CAK. Ref.27
Mutagenesis141T → A: 2-fold increase in activity. Ref.11
Mutagenesis151Y → F: 2-fold increase in activity. Ref.11
Mutagenesis88 – 892KK → EV: Reduced phosphorylation by CAK.
Mutagenesis1601T → A: Abolishes activity. Ref.11
Mutagenesis1661L → R: Reduced phosphorylation by CAK and reduced kinase activity. Ref.27
Sequence conflict8 – 125EKIGE → AQIGQ in BAA32794. Ref.5
Sequence conflict25 – 295LTGEV → STGQM in BAA32794. Ref.5
Sequence conflict272 – 2776NKRISA → YKRFST in BAA32794. Ref.5
Sequence conflict286 – 2872FQ → LE in BAA32794. Ref.5

Secondary structure

............................................................. 298
Helix Strand Turn

Details...

Sequences

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

Last modified August 1, 1992. Version 2.
Checksum: F90A0F4E70910B51

FASTA29833,930
        10         20         30         40         50         60 
MENFQKVEKI GEGTYGVVYK ARNKLTGEVV ALKKIRLDTE TEGVPSTAIR EISLLKELNH 

        70         80         90        100        110        120 
PNIVKLLDVI HTENKLYLVF EFLHQDLKKF MDASALTGIP LPLIKSYLFQ LLQGLAFCHS 

       130        140        150        160        170        180 
HRVLHRDLKP QNLLINTEGA IKLADFGLAR AFGVPVRTYT HEVVTLWYRA PEILLGCKYY 

       190        200        210        220        230        240 
STAVDIWSLG CIFAEMVTRR ALFPGDSEID QLFRIFRTLG TPDEVVWPGV TSMPDYKPSF 

       250        260        270        280        290 
PKWARQDFSK VVPPLDEDGR SLLSQMLHYD PNKRISAKAA LAHPFFQDVT KPVPHLRL 

« Hide

Isoform 2 (CDK2deltaT) [UniParc].

Checksum: 50CE890992AC71EE
Show »

FASTA26430,035

References

« Hide 'large scale' references
[1]"A new human p34 protein kinase, CDK2, identified by complementation of a cdc28 mutation in Saccharomyces cerevisiae, is a homolog of Xenopus Eg1."
Elledge S.J., Spottswood M.R.
EMBO J. 10:2653-2659(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase."
Tsai L.-H., Harlow E., Meyerson M.
Nature 353:174-177(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Cloning of a human cDNA encoding a CDC2-related kinase by complementation of a budding yeast cdc28 mutation."
Ninomiya-Tsuji J., Nomoto S., Yasuda H., Reed S.I., Matsumoto K.
Proc. Natl. Acad. Sci. U.S.A. 88:9006-9010(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Sequence of deletion type cdk2 variant in human breast cancer."
Nishikawa T., Ohta T., Fukuda M., Ogata H., Okamoto K., Isohashi F., Arima K., Yamaguchi S.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
[5]"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).
[6]NIEHS SNPs program
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-290.
[7]"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).
[8]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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].
[10]"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: Placenta.
[11]"Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15."
Gu Y., Rosenblatt J., O'Morgan D.O.
EMBO J. 11:3995-4005(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-14; TYR-15 AND THR-160, MUTAGENESIS OF THR-14; TYR-15 AND THR-160.
[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]"Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1."
Harbour J.W., Luo R.X., Dei Santi A., Postigo A.A., Dean D.C.
Cell 98:859-869(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS RB1 KINASE, INTERACTION WITH CYCLIN E.
[14]"Nucleophosmin/B23 is a target of CDK2/cyclin E in centrosome duplication."
Okuda M., Horn H.F., Tarapore P., Tokuyama Y., Smulian A.G., Chan P.K., Knudsen E.S., Hofmann I.A., Snyder J.D., Bove K.E., Fukasawa K.
Cell 103:127-140(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS NPM1 KINASE.
[15]"NPAT links cyclin E-Cdk2 to the regulation of replication-dependent histone gene transcription."
Zhao J., Kennedy B.K., Lawrence B.D., Barbie D.A., Matera A.G., Fletcher J.A., Harlow E.
Genes Dev. 14:2283-2297(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS NPAT KINASE.
[16]"Cell cycle-regulated phosphorylation of p220(NPAT) by cyclin E/Cdk2 in Cajal bodies promotes histone gene transcription."
Ma T., Van Tine B.A., Wei Y., Garrett M.D., Nelson D., Adams P.D., Wang J., Qin J., Chow L.T., Harper J.W.
Genes Dev. 14:2298-2313(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS NPAT KINASE, SUBCELLULAR LOCATION.
[17]"The C-terminal regulatory domain of p53 contains a functional docking site for cyclin A."
Luciani M.G., Hutchins J.R.A., Zheleva D., Hupp T.R.
J. Mol. Biol. 300:503-518(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS P53/TP53 KINASE, INTERACTION WITH CYCLIN A AND CYCLIN B1.
[18]"Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop."
Garrett S., Barton W.A., Knights R., Jin P., Morgan D.O., Fisher R.P.
Mol. Cell. Biol. 21:88-99(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CDK7 KINASE, PHOSPHORYLATION BY CDK7.
[19]"Characterization and expression of mammalian cyclin b3, a prepachytene meiotic cyclin."
Nguyen T.B., Manova K., Capodieci P., Lindon C., Bottega S., Wang X.-Y., Refik-Rogers J., Pines J., Wolgemuth D.J., Koff A.
J. Biol. Chem. 277:41960-41969(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CCNB3.
[20]"Human Speedy: a novel cell cycle regulator that enhances proliferation through activation of Cdk2."
Porter L.A., Dellinger R.W., Tynan J.A., Barnes E.A., Kong M., Lenormand J.-L., Donoghue D.J.
J. Cell Biol. 157:357-366(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPDYA.
[21]"Human Spy1 promotes survival of mammalian cells following DNA damage."
Barnes E.A., Porter L.A., Lenormand J.-L., Dellinger R.W., Donoghue D.J.
Cancer Res. 63:3701-3707(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPDYA.
[22]"Spy1 interacts with p27Kip1 to allow G1/S progression."
Porter L.A., Kong-Beltran M., Donoghue D.J.
Mol. Biol. Cell 14:3664-3674(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPDYA, IDENTIFICATION IN A COMPLEX WITH CDKN1B AND SPDYA.
[23]"NIRF induces G1 arrest and associates with Cdk2."
Li Y., Mori T., Hata H., Homma Y., Kochi H.
Biochem. Biophys. Res. Commun. 319:464-468(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UHRF2, IDENTIFICATION IN A COMPLEX WITH UHRF2 AND CCNE1.
[24]"p42, a novel cyclin-dependent kinase-activating kinase in mammalian cells."
Liu Y., Wu C., Galaktionov K.
J. Biol. Chem. 279:4507-4514(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-160.
[25]"Identification and comparative analysis of multiple mammalian Speedy/Ringo proteins."
Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J.
Cell Cycle 4:155-165(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPDYA AND SPDYC.
[26]"CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair."
Esashi F., Christ N., Gannon J., Liu Y., Hunt T., Jasin M., West S.C.
Nature 434:598-604(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS BRCA2 KINASE.
[27]"Recognition of Cdk2 by Cdk7."
Lolli G., Johnson L.N.
Proteins 67:1048-1059(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CAK, MUTAGENESIS OF LYS-9; 88-LYS-LYS-89 AND LEU-166, INTERACTION WITH CDK7.
[28]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"Cyclin A/cdk2 coordinates centrosomal and nuclear mitotic events."
De Boer L., Oakes V., Beamish H., Giles N., Stevens F., Somodevilla-Torres M., Desouza C., Gabrielli B.
Oncogene 27:4261-4268(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MITOSE REGULATION, SUBCELLULAR LOCATION.
[30]"Identification and characterization of CAC1 as a novel CDK2-associated cullin."
Kong Y., Nan K., Yin Y.
Cell Cycle 8:3544-3553(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CACUL1.
[31]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"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 TYR-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[33]"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].
[34]"Nuclear targeting of cyclin-dependent kinase 2 reveals essential roles of cyclin-dependent kinase 2 localization and cyclin E in vitamin D-mediated growth inhibition."
Flores O., Wang Z., Knudsen K.E., Burnstein K.L.
Endocrinology 151:896-908(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN VITAMIN D-MEDIATED GROWTH INHIBITION, SUBCELLULAR LOCATION, ENZYME REGULATION, PHOSPHORYLATION AT THR-160.
[35]"Cdk2 nitrosylation and loss of mitochondrial potential mediate NO-dependent biphasic effect on HL-60 cell cycle."
Kumar S., Barthwal M.K., Dikshit M.
Free Radic. Biol. Med. 48:851-861(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, S-NITROSYLATION.
[36]"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: PHOSPHORYLATION AT THR-160 BY CAK, DEPHOSPHORYLATION BY CDC25A.
[37]"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.
[38]"Cdk2 is required for p53-independent G2/M checkpoint control."
Chung J.H., Bunz F.
PLoS Genet. 6:E1000863-E1000863(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA DAMAGE CHECKPOINT.
[39]"Phosphorylation by Cdk2 is required for Myc to repress Ras-induced senescence in cotransformation."
Hydbring P., Bahram F., Su Y., Tronnersjoe S., Hoegstrand K., von der Lehr N., Sharifi H.R., Lilischkis R., Hein N., Wu S., Vervoorts J., Henriksson M., Grandien A., Luescher B., Larsson L.-G.
Proc. Natl. Acad. Sci. U.S.A. 107:58-63(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS MYC KINASE.
[40]"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].
[41]"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.
[42]"Compartmentalized CDK2 is connected with SHP-1 and beta-catenin and regulates insulin internalization."
Fiset A., Xu E., Bergeron S., Marette A., Pelletier G., Siminovitch K.A., Olivier M., Beauchemin N., Faure R.L.
Cell. Signal. 23:911-919(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CTNNB1 KINASE, SUBCELLULAR LOCATION, INTERACTION WITH PTPN6 AND CTNNB1.
[43]"Discovery of a novel class of 2-aminopyrimidines as CDK1 and CDK2 inhibitors."
Lee J., Kim K.H., Jeong S.
Bioorg. Med. Chem. Lett. 21:4203-4205(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITORS.
[44]"Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry."
Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G., Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.
Mol. Cell 42:511-523(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS USP37 KINASE.
[45]"An important role for CDK2 in G1 to S checkpoint activation and DNA damage response in human embryonic stem cells."
Neganova I., Vilella F., Atkinson S.P., Lloret M., Passos J.F., von Zglinicki T., O'Connor J.-E., Burks D., Jones R., Armstrong L., Lako M.
Stem Cells 29:651-659(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL CYCLE REGULATION.
[46]"A dual role of Cdk2 in DNA damage response."
Satyanarayana A., Kaldis P.
Cell Div. 4:9-9(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON DNA REPAIR, INTERACTION WITH CDKN1A/P21.
[47]"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, INHIBITORS, GENE FAMILY.
[48]"Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms."
Satyanarayana A., Kaldis P.
Oncogene 28:2925-2939(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, GENE FAMILY.
[49]"Tipping the balance: Cdk2 enables Myc to suppress senescence."
Hydbring P., Larsson L.-G.
Cancer Res. 70:6687-6691(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON SENESCENCE.
[50]"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 INHIBITORS.
[51]"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].
[52]"Crystal structure of cyclin-dependent kinase 2."
de Bondt H.L., Rosenblatt J., Jancarik J., Jones H.D., Morgan D.O., Kim S.-H.
Nature 363:595-602(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[53]"Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex."
Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J., Massague J., Pavletich N.P.
Nature 376:313-320(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CYCLIN A.
[54]"Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1."
Bourne Y., Watson M.H., Hickey M.J., Holmes W., Rocque W., Reed S.I., Tainer J.A.
Cell 84:863-874(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITG CKS1.
[55]"High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design."
Schulze-Gahmen U., de Bondt H.L., Kim S.-H.
J. Med. Chem. 39:4540-4546(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[56]"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex."
Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.
Nature 382:325-331(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CG2A AND KIP1.
[57]"Structural basis of cyclin-dependent kinase activation by phosphorylation."
Russo A.A., Jeffrey P.D., Pavletich N.P.
Nat. Struct. Biol. 3:696-700(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CG2A.
[58]"Structural basis for specificity and potency of a flavonoid inhibitor of human CDK2, a cell cycle kinase."
de Azevedo W.F. Jr., Mueller-Dieckmann H.-J., Schulze-Gahmen U., Worland P.J., Sausville E., Kim S.-H.
Proc. Natl. Acad. Sci. U.S.A. 93:2735-2740(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEX WITH L868276.
[59]"Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2."
Lawrie A.M., Noble M.E.M., Tunnah P., Brown N.R., Johnson L.N., Endicott J.A.
Nat. Struct. Biol. 4:796-801(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH STAUROSPORINE, ENZYME REGULATION.
[60]"Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors."
Gray N.S., Wodicka L., Thunnissen A.-M.W.H., Norman T.C., Kwon S., Espinoza F.H., Morgan D.O., Barnes G., Leclerc S., Meijer L., Kim S.H., Lockhart D.J., Schultz P.G.
Science 281:533-538(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
[61]"Triazolo[1,5-a]pyrimidines as novel CDK2 inhibitors: protein structure-guided design and SAR."
Richardson C.M., Williamson D.S., Parratt M.J., Borgognoni J., Cansfield A.D., Dokurno P., Francis G.L., Howes R., Moore J.D., Murray J.B., Robertson A., Surgenor A.E., Torrance C.J.
Bioorg. Med. Chem. Lett. 16:1353-1357(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS, PHOSPHORYLATION AT THR-160.
[62]"Discovery of a potent CDK2 inhibitor with a novel binding mode, using virtual screening and initial, structure-guided lead scoping."
Richardson C.M., Nunns C.L., Williamson D.S., Parratt M.J., Dokurno P., Howes R., Borgognoni J., Drysdale M.J., Finch H., Hubbard R.E., Jackson P.S., Kierstan P., Lentzen G., Moore J.D., Murray J.B., Simmonite H., Surgenor A.E., Torrance C.J.
Bioorg. Med. Chem. Lett. 17:3880-3885(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH INHIBITORS, PHOSPHORYLATION AT THR-160.
[63]"Cyclin B and cyclin A confer different substrate recognition properties on CDK2."
Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R., Johnson L.N.
Cell Cycle 6:1350-1359(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-288 IN COMPLEX WITH CCNB1, FUNCTION.
[64]"How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A."
Welburn J.P.I., Tucker J.A., Johnson T., Lindert L., Morgan M., Willis A., Noble M.E.M., Endicott J.A.
J. Biol. Chem. 282:3173-3181(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ATP, PHOSPHORYLATION AT THR-14; TYR-15 AND THR-160.
[65]"Structure-guided discovery of cyclin-dependent kinase inhibitors."
Fischmann T.O., Hruza A., Duca J.S., Ramanathan L., Mayhood T., Windsor W.T., Le H.V., Guzi T.J., Dwyer M.P., Paruch K., Doll R.J., Lees E., Parry D., Seghezzi W., Madison V.
Biopolymers 89:372-379(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[66]"Identification of N-(4-piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H-pyrazole-3-carboxamide (AT7519), a novel cyclin dependent kinase inhibitor using fragment-based X-ray crystallography and structure based drug design."
Wyatt P.G., Woodhead A.J., Berdini V., Boulstridge J.A., Carr M.G., Cross D.M., Davis D.J., Devine L.A., Early T.R., Feltell R.E., Lewis E.J., McMenamin R.L., Navarro E.F., O'Brien M.A., O'Reilly M., Reule M., Saxty G., Seavers L.C. expand/collapse author list , Smith D.M., Squires M.S., Trewartha G., Walker M.T., Woolford A.J.
J. Med. Chem. 51:4986-4999(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[67]"Briefly bound to activate: transient binding of a second catalytic magnesium activates the structure and dynamics of CDK2 kinase for catalysis."
Bao Z.Q., Jacobsen D.M., Young M.A.
Structure 19:675-690(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 1-296 IN COMPLEX WITH ATP AND MAGNESIUM, PHOSPHORYLATION AT THR-160.
[68]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-45 AND SER-290.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61622 mRNA. Translation: CAA43807.1.
X62071 mRNA. Translation: CAA43985.1.
M68520 mRNA. Translation: AAA35667.1.
AB012305 mRNA. Translation: BAA32794.1.
BT006821 mRNA. Translation: AAP35467.1.
AF512553 Genomic DNA. Translation: AAM34794.1.
AK291941 mRNA. Translation: BAF84630.1.
AC025162 Genomic DNA. No translation available.
AC034102 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96858.1.
BC003065 mRNA. Translation: AAH03065.1.
PIRA41227.
RefSeqNP_001789.2. NM_001798.3.
NP_439892.2. NM_052827.2.
UniGeneHs.19192.
Hs.689624.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQ1X-ray2.00A1-298[»]
1B38X-ray2.00A1-298[»]
1B39X-ray2.10A1-298[»]
1BUHX-ray2.60A1-298[»]
1CKPX-ray2.05A1-298[»]
1DI8X-ray2.20A1-298[»]
1DM2X-ray2.10A1-298[»]
1E1VX-ray1.95A1-298[»]
1E1XX-ray1.85A1-298[»]
1E9HX-ray2.50A/C1-296[»]
1F5QX-ray2.50A/C1-298[»]
1FINX-ray2.30A/C1-298[»]
1FQ1X-ray3.00B1-298[»]
1FVTX-ray2.20A1-298[»]
1FVVX-ray2.80A/C1-298[»]
1G5SX-ray2.61A1-298[»]
1GIHX-ray2.80A1-298[»]
1GIIX-ray2.00A1-298[»]
1GIJX-ray2.20A1-298[»]
1GY3X-ray2.70A/C1-296[»]
1GZ8X-ray1.30A1-298[»]
1H00X-ray1.60A1-298[»]
1H01X-ray1.79A1-298[»]
1H07X-ray1.85A1-298[»]
1H08X-ray1.80A1-298[»]
1H0VX-ray1.90A1-298[»]
1H0WX-ray2.10A1-298[»]
1H1PX-ray2.10A/C1-298[»]
1H1QX-ray2.50A/C1-298[»]
1H1RX-ray2.00A/C1-298[»]
1H1SX-ray2.00A/C1-298[»]
1H24X-ray2.50A/C1-298[»]
1H25X-ray2.50A/C1-298[»]
1H26X-ray2.24A/C1-298[»]
1H27X-ray2.20A/C1-298[»]
1H28X-ray2.80A/C1-298[»]
1HCKX-ray1.90A1-298[»]
1HCLX-ray1.80A1-298[»]
1JSTX-ray2.60A/C1-298[»]
1JSUX-ray2.30A1-298[»]
1JSVX-ray1.96A1-298[»]
1JVPX-ray1.53P1-298[»]
1KE5X-ray2.20A1-298[»]
1KE6X-ray2.00A1-298[»]
1KE7X-ray2.00A1-298[»]
1KE8X-ray2.00A1-298[»]
1KE9X-ray2.00A1-298[»]
1OGUX-ray2.60A/C1-298[»]
1OI9X-ray2.10A/C1-298[»]
1OIQX-ray2.31A1-298[»]
1OIRX-ray1.91A1-298[»]
1OITX-ray1.60A1-298[»]
1OIUX-ray2.00A/C1-298[»]
1OIYX-ray2.40A/C1-298[»]
1OKVX-ray2.40A/C1-298[»]
1OKWX-ray2.50A/C1-298[»]
1OL1X-ray2.90A/C1-298[»]
1OL2X-ray2.60A/C1-298[»]
1P2AX-ray2.50A1-298[»]
1P5EX-ray2.22A/C1-298[»]
1PF8X-ray2.51A1-298[»]
1PKDX-ray2.30A/C1-296[»]
1PW2X-ray1.95A1-298[»]
1PXIX-ray1.95A1-298[»]
1PXJX-ray2.30A1-298[»]
1PXKX-ray2.80A1-298[»]
1PXLX-ray2.50A1-298[»]
1PXMX-ray2.53A1-298[»]
1PXNX-ray2.50A1-298[»]
1PXOX-ray1.96A1-298[»]
1PXPX-ray2.30A1-298[»]
1PYEX-ray2.00A1-298[»]
1QMZX-ray2.20A/C1-298[»]
1R78X-ray2.00A1-298[»]
1URCX-ray2.60A/C1-298[»]
1URWX-ray1.60A1-298[»]
1V1KX-ray2.31A1-298[»]
1VYWX-ray2.30A/C1-298[»]
1VYZX-ray2.21A1-298[»]
1W0XX-ray2.20C1-298[»]
1W8CX-ray2.05A1-298[»]
1W98X-ray2.15A1-297[»]
1WCCX-ray2.20A1-298[»]
1Y8YX-ray2.00A1-298[»]
1Y91X-ray2.15A1-298[»]
1YKRX-ray1.80A1-298[»]
2A0CX-ray1.95X1-298[»]
2A4LX-ray2.40A1-298[»]
2B52X-ray1.88A1-298[»]
2B53X-ray2.00A1-298[»]
2B54X-ray1.85A1-298[»]
2B55X-ray1.85A1-298[»]
2BHEX-ray1.90A1-298[»]
2BHHX-ray2.60A1-298[»]
2BKZX-ray2.60A/C1-298[»]
2BPMX-ray2.40A/C1-298[»]
2BTRX-ray1.85A1-298[»]
2BTSX-ray1.99A1-298[»]
2C4GX-ray2.70A/C1-298[»]
2C5NX-ray2.10A/C1-298[»]
2C5OX-ray2.10A/C1-298[»]
2C5VX-ray2.90A/C1-298[»]
2C5XX-ray2.90A/C1-298[»]
2C5YX-ray2.25A1-298[»]
2C68X-ray1.95A1-298[»]
2C69X-ray2.10A1-298[»]
2C6IX-ray1.80A1-298[»]
2C6KX-ray1.90A1-298[»]
2C6LX-ray2.30A1-298[»]
2C6MX-ray1.90A1-298[»]
2C6OX-ray2.10A1-298[»]
2C6TX-ray2.61A/C1-298[»]
2CCHX-ray1.70A/C1-298[»]
2CCIX-ray2.70A/C1-298[»]
2CJMX-ray2.30A/C1-298[»]
2CLXX-ray1.80A1-298[»]
2DS1X-ray2.00A1-298[»]
2DUVX-ray2.20A1-298[»]
2EXMX-ray1.80A1-298[»]
2FVDX-ray1.85A1-298[»]
2G9XX-ray2.50A/C1-298[»]
2HICmodel-A1-298[»]
2I40X-ray2.80A/C1-298[»]
2IW6X-ray2.30A/C1-298[»]
2IW8X-ray2.30A/C1-298[»]
2IW9X-ray2.00A/C1-298[»]
2J9MX-ray2.50A1-298[»]
2JGZX-ray2.90A1-288[»]
2R3FX-ray1.50A1-298[»]
2R3GX-ray1.55A1-298[»]
2R3HX-ray1.50A1-298[»]
2R3IX-ray1.28A1-298[»]
2R3JX-ray1.65A1-298[»]
2R3KX-ray1.70A1-298[»]
2R3LX-ray1.65A1-298[»]
2R3MX-ray1.70A1-298[»]
2R3NX-ray1.63A1-298[»]
2R3OX-ray1.80A1-298[»]
2R3PX-ray1.66A1-298[»]
2R3QX-ray1.35A1-298[»]
2R3RX-ray1.47A1-298[»]
2R64X-ray2.30A1-298[»]
2UUEX-ray2.06A/C1-298[»]
2UZBX-ray2.70A/C1-298[»]
2UZDX-ray2.72A/C1-298[»]
2UZEX-ray2.40A/C1-298[»]
2UZLX-ray2.40A/C1-298[»]
2UZNX-ray2.30A1-298[»]
2UZOX-ray2.30A1-298[»]
2V0DX-ray2.20A1-298[»]
2V22X-ray2.60A/C1-298[»]
2VTAX-ray2.00A1-298[»]
2VTHX-ray1.90A1-298[»]
2VTIX-ray2.00A1-298[»]
2VTJX-ray2.20A1-298[»]
2VTLX-ray2.00A1-298[»]
2VTMX-ray2.25A1-298[»]
2VTNX-ray2.20A1-298[»]
2VTOX-ray2.19A1-298[»]
2VTPX-ray2.15A1-298[»]
2VTQX-ray1.90A1-298[»]
2VTRX-ray1.90A1-298[»]
2VTSX-ray1.90A1-298[»]
2VTTX-ray1.68A1-298[»]
2VU3X-ray1.85A1-298[»]
2VV9X-ray1.90A1-298[»]
2W05X-ray1.90A1-298[»]
2W06X-ray2.04A1-298[»]
2W17X-ray2.15A1-298[»]
2W1HX-ray2.15A1-298[»]
2WEVX-ray2.30A/C1-298[»]
2WFYX-ray2.53A/C1-298[»]
2WHBX-ray2.90A/C1-298[»]
2WIHX-ray2.50A/C1-298[»]
2WIPX-ray2.80A/C1-298[»]
2WMAX-ray2.80A/C1-298[»]
2WMBX-ray2.60A/C1-298[»]
2WPAX-ray2.51A/C1-298[»]
2WXVX-ray2.60A/C1-298[»]
2X1NX-ray2.75A/C1-298[»]
2XMYX-ray1.90A1-298[»]
2XNBX-ray1.85A1-298[»]
3BHTX-ray2.00A/C1-298[»]
3BHUX-ray2.30A/C1-298[»]
3BHVX-ray2.10A/C1-298[»]
3DDPX-ray2.70A/C1-298[»]
3DDQX-ray1.80A/C1-298[»]
3DOGX-ray2.70A/C1-298[»]
3EIDX-ray3.15A/C1-298[»]
3EJ1X-ray3.22A/C1-298[»]
3EOCX-ray3.20A/C1-298[»]
3EZRX-ray1.90A1-298[»]
3EZVX-ray1.99A1-298[»]
3F5XX-ray2.40A/C1-298[»]
3FZ1X-ray1.90A1-298[»]
3IG7X-ray1.80A1-298[»]
3IGGX-ray1.80A1-298[»]
3LE6X-ray2.00A1-298[»]
3LFNX-ray2.28A1-298[»]
3LFQX-ray2.03A1-298[»]
3LFSX-ray2.40A1-298[»]
3MY5X-ray2.10A/C1-298[»]
3NS9X-ray1.78A1-298[»]
3PJ8X-ray1.96A1-298[»]
3PXFX-ray1.80A1-298[»]
3PXQX-ray1.90A1-298[»]
3PXRX-ray2.00A1-298[»]
3PXYX-ray1.80A1-298[»]
3PXZX-ray1.70A1-298[»]
3PY0X-ray1.75A1-298[»]
3PY1X-ray2.05A1-298[»]
3QHRX-ray2.17A/C1-296[»]
3QHWX-ray1.91A/C1-296[»]
3QL8X-ray1.90A1-298[»]
3QQFX-ray1.75A1-298[»]
3QQGX-ray1.90A1-298[»]
3QQHX-ray1.87A1-298[»]
3QQJX-ray1.70A1-298[»]
3QQKX-ray1.86A1-298[»]
3QQLX-ray1.85A1-298[»]
3QRTX-ray1.75A1-298[»]
3QRUX-ray1.95A1-298[»]
3QTQX-ray1.80A1-298[»]
3QTRX-ray1.85A1-298[»]
3QTSX-ray1.90A1-298[»]
3QTUX-ray1.82A1-298[»]
3QTWX-ray1.85A1-298[»]
3QTXX-ray1.95A1-298[»]
3QTZX-ray2.00A1-298[»]
3QU0X-ray1.95A1-298[»]
3QWJX-ray1.75A1-298[»]
3QWKX-ray1.85A1-298[»]
3QX2X-ray1.75A1-298[»]
3QX4X-ray1.92A1-298[»]
3QXOX-ray1.75A1-298[»]
3QXPX-ray1.75A1-298[»]
3QZFX-ray2.00A1-298[»]
3QZGX-ray1.75A1-298[»]
3QZHX-ray1.95A1-298[»]
3QZIX-ray1.75A1-298[»]
3R1QX-ray1.85A1-298[»]
3R1SX-ray1.80A1-298[»]
3R1YX-ray1.80A1-298[»]
3R28X-ray1.75A1-298[»]
3R6XX-ray1.75A1-298[»]
3R71X-ray1.75A1-298[»]
3R73X-ray1.70A1-298[»]
3R7EX-ray1.90A1-298[»]
3R7IX-ray1.85A1-298[»]
3R7UX-ray1.75A1-298[»]
3R7VX-ray1.95A1-298[»]
3R7YX-ray1.90A1-298[»]
3R83X-ray1.75A1-298[»]
3R8LX-ray1.90A1-298[»]
3R8MX-ray1.80A1-298[»]
3R8PX-ray1.80A1-298[»]
3R8UX-ray2.00A1-298[»]
3R8VX-ray1.90A1-298[»]
3R8ZX-ray1.85A1-298[»]
3R9DX-ray1.95A1-298[»]
3R9HX-ray2.10A1-298[»]
3R9NX-ray1.75A1-298[»]
3R9OX-ray1.90A1-298[»]
3RAHX-ray1.75A1-298[»]
3RAIX-ray1.70A1-298[»]
3RAKX-ray1.75A1-298[»]
3RALX-ray1.75A1-298[»]
3RJCX-ray1.85A1-298[»]
3RK5X-ray2.00A1-298[»]
3RK7X-ray1.80A1-298[»]
3RK9X-ray1.85A1-298[»]
3RKBX-ray2.00A1-298[»]
3RM6X-ray1.60A1-298[»]
3RM7X-ray1.85A1-298[»]
3RMFX-ray1.75A1-298[»]
3RNIX-ray1.95A1-298[»]
3ROYX-ray1.75A1-298[»]
3RPOX-ray1.75A1-298[»]
3RPRX-ray1.75A1-298[»]
3RPVX-ray1.80A1-298[»]
3RPYX-ray1.90A1-298[»]
3RZBX-ray1.90A1-298[»]
3S00X-ray1.80A1-298[»]
3S0OX-ray2.00A1-298[»]
3S1HX-ray1.75A1-298[»]
3S2PX-ray2.30A1-298[»]
3SQQX-ray1.85A1-298[»]
3SW4X-ray1.70A1-298[»]
3SW7X-ray1.80A1-298[»]
3TI1X-ray1.99A1-298[»]
3TIYX-ray1.84A1-298[»]
3TIZX-ray2.02A1-298[»]
3TNWX-ray2.00A/C1-298[»]
3ULIX-ray2.00A1-298[»]
3UNJX-ray1.90A1-298[»]
3UNKX-ray2.10A1-298[»]
3WBLX-ray2.00A1-298[»]
4ACMX-ray1.63A1-298[»]
4BCKX-ray2.05A/C1-298[»]
4BCMX-ray2.45A/C1-298[»]
4BCNX-ray2.10A/C1-298[»]
4BCOX-ray2.05A/C1-298[»]
4BCPX-ray2.26A/C1-298[»]
4BCQX-ray2.40A/C1-298[»]
4BGHX-ray1.95A1-298[»]
4CFNX-ray2.20A/C1-298[»]
4CFWX-ray2.45A/C1-298[»]
4EK3X-ray1.34A1-298[»]
4EK4X-ray1.26A1-298[»]
4EK5X-ray1.60A1-298[»]
4EK6X-ray1.52A1-298[»]
4EK8X-ray1.70A1-298[»]
4EOIX-ray2.00A/C1-298[»]
4EOJX-ray1.65A/C1-298[»]
4EOKX-ray2.57A/C1-297[»]
4EOLX-ray2.40A/C1-297[»]
4EOMX-ray2.10A/C1-297[»]
4EONX-ray2.40A/C1-298[»]
4EOOX-ray2.10A/C1-297[»]
4EOPX-ray1.99A/C1-297[»]
4EOQX-ray2.15A/C1-297[»]
4EORX-ray2.20A/C1-297[»]
4EOSX-ray2.57A/C1-297[»]
4ERWX-ray2.00A1-298[»]
4EZ3X-ray2.00A1-298[»]
4EZ7X-ray2.49A1-298[»]
4FKGX-ray1.51A1-298[»]
4FKIX-ray1.60A1-298[»]
4FKJX-ray1.63A1-298[»]
4FKLX-ray1.26A1-298[»]
4FKOX-ray1.55A1-298[»]
4FKPX-ray1.60A1-298[»]
4FKQX-ray1.75A1-298[»]
4FKRX-ray1.90A1-298[»]
4FKSX-ray1.55A1-298[»]
4FKTX-ray1.60A1-298[»]
4FKUX-ray1.47A1-298[»]
4FKVX-ray1.70A1-298[»]
4FKWX-ray1.80A1-298[»]
4FX3X-ray2.75A/C1-298[»]
4GCJX-ray1.42A1-298[»]
4I3ZX-ray2.05A/C1-296[»]
4II5X-ray2.15A/C1-298[»]
4KD1X-ray1.70A1-298[»]
4LYNX-ray2.00A1-298[»]
4NJ3X-ray1.85A1-298[»]
ProteinModelPortalP24941.
SMRP24941. Positions 1-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107452. 628 interactions.
DIPDIP-161N.
IntActP24941. 62 interactions.
MINTMINT-96328.
STRING9606.ENSP00000266970.

Chemistry

BindingDBP24941.
ChEMBLCHEMBL1907605.
GuidetoPHARMACOLOGY1973.

PTM databases

PhosphoSiteP24941.

Polymorphism databases

DMDM116051.

Proteomic databases

PaxDbP24941.
PRIDEP24941.

Protocols and materials databases

DNASU1017.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266970; ENSP00000266970; ENSG00000123374. [P24941-1]
ENST00000354056; ENSP00000243067; ENSG00000123374. [P24941-2]
GeneID1017.
KEGGhsa:1017.
UCSCuc001sit.4. human. [P24941-1]
uc001siu.4. human. [P24941-2]

Organism-specific databases

CTD1017.
GeneCardsGC12P056360.
HGNCHGNC:1771. CDK2.
HPACAB013115.
MIM116953. gene.
neXtProtNX_P24941.
PharmGKBPA101.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidP24941.
KOK02206.
OrthoDBEOG7966H8.
PhylomeDBP24941.
TreeFamTF101021.

Enzyme and pathway databases

BRENDA2.7.11.22. 2681.
ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.
REACT_604. Hemostasis.
SignaLinkP24941.

Gene expression databases

ArrayExpressP24941.
BgeeP24941.
CleanExHS_CDK2.
GenevestigatorP24941.

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

ChiTaRSCDK2. human.
EvolutionaryTraceP24941.
GeneWikiCyclin-dependent_kinase_2.
GenomeRNAi1017.
NextBio4273.
PROP24941.
SOURCESearch...

Entry information

Entry nameCDK2_HUMAN
AccessionPrimary (citable) accession number: P24941
Secondary accession number(s): A8K7C6, O75100
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 185 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM